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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Dynein light chain 1, cytoplasmic''' is a [[protein]] that in humans is encoded by the ''DYNLL1'' [[gene]].<ref name="pmid8628263">{{cite journal | vauthors = Dick T, Ray K, Salz HK, Chia W | title = Cytoplasmic dynein (ddlc1) mutations cause morphogenetic defects and apoptotic cell death in Drosophila melanogaster | journal = Molecular and Cellular Biology | volume = 16 | issue = 5 | pages = 1966–77 | date = May 1996 | pmid = 8628263 | pmc = 231184 | doi =  10.1128/mcb.16.5.1966}}</ref><ref name="pmid8864115">{{cite journal | vauthors = Jaffrey SR, Snyder SH | title = PIN: an associated protein inhibitor of neuronal nitric oxide synthase | journal = Science | volume = 274 | issue = 5288 | pages = 774–7 | date = Nov 1996 | pmid = 8864115 | pmc =  | doi = 10.1126/science.274.5288.774 }}</ref><ref name="pmid16260502">{{cite journal | vauthors = Pfister KK, Fisher EM, Gibbons IR, Hays TS, Holzbaur EL, McIntosh JR, Porter ME, Schroer TA, Vaughan KT, Witman GB, King SM, Vallee RB | title = Cytoplasmic dynein nomenclature | journal = The Journal of Cell Biology | volume = 171 | issue = 3 | pages = 411–3 | date = Nov 2005 | pmid = 16260502 | pmc = 2171247 | doi = 10.1083/jcb.200508078 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: DYNLL1 dynein, light chain, LC8-type 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8655| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_DYNLL1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1cmi.
| PDB = {{PDB2|1cmi}}, {{PDB2|1f3c}}, {{PDB2|1f95}}, {{PDB2|1f96}}, {{PDB2|1pwj}}, {{PDB2|1pwk}}, {{PDB2|1re6}}, {{PDB2|1rhw}}, {{PDB2|2pg1}}
| Name = Dynein, light chain, LC8-type 1
| HGNCid = 15476
| Symbol = DYNLL1
| AltSymbols =; DLC1; DLC8; DNCL1; DNCLC1; LC8; LC8a; MGC126137; MGC126138; PIN; hdlc1
| OMIM = 601562
| ECnumber = 
| Homologene = 37844
| MGIid = 1861457
| GeneAtlas_image1 = PBB_GE_DYNLL1_200703_at_tn.png
| Function = {{GNF_GO|id=GO:0003777 |text = microtubule motor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005868 |text = cytoplasmic dynein complex}} {{GNF_GO|id=GO:0005874 |text = microtubule}}
| Process = {{GNF_GO|id=GO:0007017 |text = microtubule-based process}} {{GNF_GO|id=GO:0007292 |text = female gamete generation}} {{GNF_GO|id=GO:0009653 |text = anatomical structure morphogenesis}} {{GNF_GO|id=GO:0030036 |text = actin cytoskeleton organization and biogenesis}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 8655
    | Hs_Ensembl = ENSG00000088986
    | Hs_RefseqProtein = NP_001032583
    | Hs_RefseqmRNA = NM_001037494
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 12
    | Hs_GenLoc_start = 119418309
    | Hs_GenLoc_end = 119420679
    | Hs_Uniprot = P63167
    | Mm_EntrezGene = 56455
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = NM_019682
    | Mm_RefseqProtein = NP_062656
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Dynein, light chain, LC8-type 1''', also known as '''DYNLL1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DYNLL1 dynein, light chain, LC8-type 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8655| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
Cytoplasmic dyneins are large enzyme complexes with a molecular mass of about 1,200 kD. They contain two force-producing heads formed primarily from dynein heavy chains, and stalks linking the heads to a basal domain, which contains a varying number of accessory intermediate chains. The complex is involved in intracellular transport and motility. The protein described in this record is a light chain and exists as part of this complex but also physically interacts with and inhibits the activity of neuronal nitric oxide synthase. Binding of this protein destabilizes the neuronal nitric oxide synthase dimer, a conformation necessary for activity, and it may regulate numerous biologic processes through its effects on nitric oxide synthase activity. Alternate transcriptional splice variants have been characterized.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = Cytoplasmic dyneins are large enzyme complexes with a molecular mass of about 1,200 kD. They contain two force-producing heads formed primarily from dynein heavy chains, and stalks linking the heads to a basal domain, which contains a varying number of accessory intermediate chains. The complex is involved in intracellular transport and motility. The protein described in this record is a light chain and exists as part of this complex but also physically interacts with and inhibits the activity of neuronal nitric oxide synthase. Binding of this protein destabilizes the neuronal nitric oxide synthase dimer, a conformation necessary for activity, and it may regulate numerous biologic processes through its effects on nitric oxide synthase activity. Alternate transcriptional splice variants have been characterized.<ref name="entrez">{{cite web | title = Entrez Gene: DYNLL1 dynein, light chain, LC8-type 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8655| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
DYNLL1 has been shown to [[Protein-protein interaction|interact]] with:
{{div col|colwidth=20em}}
* [[BCL2L11]],<ref name = pmid14561217>{{cite journal | vauthors = Day CL, Puthalakath H, Skea G, Strasser A, Barsukov I, Lian LY, Huang DC, Hinds MG | title = Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands | journal = The Biochemical Journal | volume = 377 | issue = Pt 3 | pages = 597–605 | date = Feb 2004 | pmid = 14561217 | pmc = 1223895 | doi = 10.1042/BJ20031251 }}</ref><ref name = pmid15193260>{{cite journal | vauthors = Vadlamudi RK, Bagheri-Yarmand R, Yang Z, Balasenthil S, Nguyen D, Sahin AA, den Hollander P, Kumar R | title = Dynein light chain 1, a p21-activated kinase 1-interacting substrate, promotes cancerous phenotypes | journal = Cancer Cell | volume = 5 | issue = 6 | pages = 575–85 | date = Jun 2004 | pmid = 15193260 | doi = 10.1016/j.ccr.2004.05.022 }}</ref>
* [[DLG4]]<ref name = pmid10844022/>
* [[DLGAP1]],<ref name = pmid10844022>{{cite journal | vauthors = Naisbitt S, Valtschanoff J, Allison DW, Sala C, Kim E, Craig AM, Weinberg RJ, Sheng M | title = Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein | journal = The Journal of Neuroscience | volume = 20 | issue = 12 | pages = 4524–34 | date = Jun 2000 | pmid = 10844022 | doi =  }}</ref>
* [[DYNC1I1]],<ref name = pmid12475239>{{cite journal | vauthors = Diefenbach RJ, Diefenbach E, Douglas MW, Cunningham AL | title = The heavy chain of conventional kinesin interacts with the SNARE proteins SNAP25 and SNAP23 | journal = Biochemistry | volume = 41 | issue = 50 | pages = 14906–15 | date = Dec 2002 | pmid = 12475239 | doi =  10.1021/bi026417u}}</ref>
* [[IκBα]],<ref name = pmid9372968>{{cite journal | vauthors = Crépieux P, Kwon H, Leclerc N, Spencer W, Richard S, Lin R, Hiscott J | title = I kappaB alpha physically interacts with a cytoskeleton-associated protein through its signal response domain | journal = Molecular and Cellular Biology | volume = 17 | issue = 12 | pages = 7375–85 | date = Dec 1997 | pmid = 9372968 | pmc = 232593 | doi =  }}</ref>
* [[MYO5A]],<ref name = pmid10844022/>
* [[NRF1]],<ref name = pmid11069771>{{cite journal | vauthors = Herzig RP, Andersson U, Scarpulla RC | title = Dynein light chain interacts with NRF-1 and EWG, structurally and functionally related transcription factors from humans and drosophila | journal = Journal of Cell Science | volume = 113 | issue =  23| pages = 4263–73 | date = Dec 2000 | pmid = 11069771 | doi =  }}</ref>
* [[PAK1]],<ref name = pmid15193260/>  and
* [[TP53BP1]].<ref name = pmid15611139>{{cite journal | vauthors = Lo KW, Kan HM, Chan LN, Xu WG, Wang KP, Wu Z, Sheng M, Zhang M | title = The 8-kDa dynein light chain binds to p53-binding protein 1 and mediates DNA damage-induced p53 nuclear accumulation | journal = The Journal of Biological Chemistry | volume = 280 | issue = 9 | pages = 8172–9 | date = Mar 2005 | pmid = 15611139 | doi = 10.1074/jbc.M411408200 }}</ref>
{{Div col end}}
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Robertson NG, Khetarpal U, Gutiérrez-Espeleta GA, Bieber FR, Morton CC | title = Isolation of novel and known genes from a human fetal cochlear cDNA library using subtractive hybridization and differential screening | journal = Genomics | volume = 23 | issue = 1 | pages = 42–50 | date = Sep 1994 | pmid = 7829101 | doi = 10.1006/geno.1994.1457 }}
| citations =
* {{cite journal | vauthors = Crépieux P, Kwon H, Leclerc N, Spencer W, Richard S, Lin R, Hiscott J | title = I kappaB alpha physically interacts with a cytoskeleton-associated protein through its signal response domain | journal = Molecular and Cellular Biology | volume = 17 | issue = 12 | pages = 7375–85 | date = Dec 1997 | pmid = 9372968 | pmc = 232593 | doi =  }}
*{{cite journal | author=Robertson NG, Khetarpal U, Gutiérrez-Espeleta GA, ''et al.'' |title=Isolation of novel and known genes from a human fetal cochlear cDNA library using subtractive hybridization and differential screening. |journal=Genomics |volume=23 |issue= 1 |pages= 42-50 |year= 1995 |pmid= 7829101 |doi= 10.1006/geno.1994.1457 }}
* {{cite journal | vauthors = Tochio H, Ohki S, Zhang Q, Li M, Zhang M | title = Solution structure of a protein inhibitor of neuronal nitric oxide synthase | journal = Nature Structural Biology | volume = 5 | issue = 11 | pages = 965–9 | date = Nov 1998 | pmid = 9808041 | doi = 10.1038/2940 }}
*{{cite journal | author=Dick T, Ray K, Salz HK, Chia W |title=Cytoplasmic dynein (ddlc1) mutations cause morphogenetic defects and apoptotic cell death in Drosophila melanogaster. |journal=Mol. Cell. Biol. |volume=16 |issue= 5 |pages= 1966-77 |year= 1996 |pmid= 8628263 |doi=  }}
* {{cite journal | vauthors = Rodríguez-Crespo I, Straub W, Gavilanes F, Ortiz de Montellano PR | title = Binding of dynein light chain (PIN) to neuronal nitric oxide synthase in the absence of inhibition | journal = Archives of Biochemistry and Biophysics | volume = 359 | issue = 2 | pages = 297–304 | date = Nov 1998 | pmid = 9808772 | doi = 10.1006/abbi.1998.0928 }}
*{{cite journal | author=Jaffrey SR, Snyder SH |title=PIN: an associated protein inhibitor of neuronal nitric oxide synthase. |journal=Science |volume=274 |issue= 5288 |pages= 774-7 |year= 1996 |pmid= 8864115 |doi= }}
* {{cite journal | vauthors = Fan JS, Zhang Q, Li M, Tochio H, Yamazaki T, Shimizu M, Zhang M | title = Protein inhibitor of neuronal nitric-oxide synthase, PIN, binds to a 17-amino acid residue fragment of the enzyme | journal = The Journal of Biological Chemistry | volume = 273 | issue = 50 | pages = 33472–81 | date = Dec 1998 | pmid = 9837926 | doi = 10.1074/jbc.273.50.33472 }}
*{{cite journal | author=Crépieux P, Kwon H, Leclerc N, ''et al.'' |title=I kappaB alpha physically interacts with a cytoskeleton-associated protein through its signal response domain. |journal=Mol. Cell. Biol. |volume=17 |issue= 12 |pages= 7375-85 |year= 1997 |pmid= 9372968 |doi= }}
* {{cite journal | vauthors = Puthalakath H, Huang DC, O'Reilly LA, King SM, Strasser A | title = The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex | journal = Molecular Cell | volume = 3 | issue = 3 | pages = 287–96 | date = Mar 1999 | pmid = 10198631 | doi = 10.1016/S1097-2765(00)80456-6 }}
*{{cite journal | author=Tochio H, Ohki S, Zhang Q, ''et al.'' |title=Solution structure of a protein inhibitor of neuronal nitric oxide synthase. |journal=Nat. Struct. Biol. |volume=5 |issue= 11 |pages= 965-9 |year= 1998 |pmid= 9808041 |doi= 10.1038/2940 }}
* {{cite journal | vauthors = Liang J, Jaffrey SR, Guo W, Snyder SH, Clardy J | title = Structure of the PIN/LC8 dimer with a bound peptide | journal = Nature Structural Biology | volume = 6 | issue = 8 | pages = 735–40 | date = Aug 1999 | pmid = 10426949 | doi = 10.1038/11501 }}
*{{cite journal | author=Rodríguez-Crespo I, Straub W, Gavilanes F, Ortiz de Montellano PR |title=Binding of dynein light chain (PIN) to neuronal nitric oxide synthase in the absence of inhibition. |journal=Arch. Biochem. Biophys. |volume=359 |issue= 2 |pages= 297-304 |year= 1998 |pmid= 9808772 |doi= }}
* {{cite journal | vauthors = Epstein E, Sela-Brown A, Ringel I, Kilav R, King SM, Benashski SE, Yisraeli JK, Silver J, Naveh-Many T | title = Dynein light chain binding to a 3'-untranslated sequence mediates parathyroid hormone mRNA association with microtubules | journal = The Journal of Clinical Investigation | volume = 105 | issue = 4 | pages = 505–12 | date = Feb 2000 | pmid = 10683380 | pmc = 289163 | doi = 10.1172/JCI8557 }}
*{{cite journal | author=Fan JS, Zhang Q, Li M, ''et al.'' |title=Protein inhibitor of neuronal nitric-oxide synthase, PIN, binds to a 17-amino acid residue fragment of the enzyme. |journal=J. Biol. Chem. |volume=273 |issue= 50 |pages= 33472-81 |year= 1999 |pmid= 9837926 |doi= }}
* {{cite journal | vauthors = Naisbitt S, Valtschanoff J, Allison DW, Sala C, Kim E, Craig AM, Weinberg RJ, Sheng M | title = Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein | journal = The Journal of Neuroscience | volume = 20 | issue = 12 | pages = 4524–34 | date = Jun 2000 | pmid = 10844022 | doi = }}
*{{cite journal | author=Puthalakath H, Huang DC, O'Reilly LA, ''et al.'' |title=The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex. |journal=Mol. Cell |volume=3 |issue= 3 |pages= 287-96 |year= 1999 |pmid= 10198631 |doi= }}
* {{cite journal | vauthors = Jacob Y, Badrane H, Ceccaldi PE, Tordo N | title = Cytoplasmic dynein LC8 interacts with lyssavirus phosphoprotein | journal = Journal of Virology | volume = 74 | issue = 21 | pages = 10217–22 | date = Nov 2000 | pmid = 11024152 | pmc = 102062 | doi = 10.1128/JVI.74.21.10217-10222.2000 }}
*{{cite journal | author=Liang J, Jaffrey SR, Guo W, ''et al.'' |title=Structure of the PIN/LC8 dimer with a bound peptide. |journal=Nat. Struct. Biol. |volume=6 |issue= 8 |pages= 735-40 |year= 1999 |pmid= 10426949 |doi= 10.1038/11501 }}
* {{cite journal | vauthors = Herzig RP, Andersson U, Scarpulla RC | title = Dynein light chain interacts with NRF-1 and EWG, structurally and functionally related transcription factors from humans and drosophila | journal = Journal of Cell Science | volume = 113 | issue = 23| pages = 4263–73 | date = Dec 2000 | pmid = 11069771 | doi =  }}
*{{cite journal | author=Epstein E, Sela-Brown A, Ringel I, ''et al.'' |title=Dynein light chain binding to a 3'-untranslated sequence mediates parathyroid hormone mRNA association with microtubules. |journal=J. Clin. Invest. |volume=105 |issue= 4 |pages= 505-12 |year= 2000 |pmid= 10683380 |doi= }}
* {{cite journal | vauthors = Haraguchi K, Satoh K, Yanai H, Hamada F, Kawabuchi M, Akiyama T | title = The hDLG-associated protein DAP interacts with dynein light chain and neuronal nitric oxide synthase | journal = Genes to Cells | volume = 5 | issue = 11 | pages = 905–911 | date = Nov 2000 | pmid = 11122378 | doi = 10.1046/j.1365-2443.2000.00374.x }}
*{{cite journal | author=Naisbitt S, Valtschanoff J, Allison DW, ''et al.'' |title=Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein. |journal=J. Neurosci. |volume=20 |issue= 12 |pages= 4524-34 |year= 2000 |pmid= 10844022 |doi=  }}
* {{cite journal | vauthors = Lo KW, Naisbitt S, Fan JS, Sheng M, Zhang M | title = The 8-kDa dynein light chain binds to its targets via a conserved (K/R)XTQT motif | journal = The Journal of Biological Chemistry | volume = 276 | issue = 17 | pages = 14059–66 | date = Apr 2001 | pmid = 11148209 | doi = 10.1074/jbc.M010320200 }}
*{{cite journal | author=Jacob Y, Badrane H, Ceccaldi PE, Tordo N |title=Cytoplasmic dynein LC8 interacts with lyssavirus phosphoprotein. |journal=J. Virol. |volume=74 |issue= 21 |pages= 10217-22 |year= 2000 |pmid= 11024152 |doi= }}
* {{cite journal | vauthors = Yano H, Lee FS, Kong H, Chuang J, Arevalo J, Perez P, Sung C, Chao MV | title = Association of Trk neurotrophin receptors with components of the cytoplasmic dynein motor | journal = The Journal of Neuroscience | volume = 21 | issue = 3 | pages = RC125 | date = Feb 2001 | pmid = 11157096 | doi =  }}
*{{cite journal | author=Herzig RP, Andersson U, Scarpulla RC |title=Dynein light chain interacts with NRF-1 and EWG, structurally and functionally related transcription factors from humans and drosophila. |journal=J. Cell. Sci. |volume=113 Pt 23 |issue= |pages= 4263-73 |year= 2001 |pmid= 11069771 |doi= }}
* {{cite journal | vauthors = Fan J, Zhang Q, Tochio H, Li M, Zhang M | title = Structural basis of diverse sequence-dependent target recognition by the 8 kDa dynein light chain | journal = Journal of Molecular Biology | volume = 306 | issue = 1 | pages = 97–108 | date = Feb 2001 | pmid = 11178896 | doi = 10.1006/jmbi.2000.4374 }}
*{{cite journal | author=Haraguchi K, Satoh K, Yanai H, ''et al.'' |title=The hDLG-associated protein DAP interacts with dynein light chain and neuronal nitric oxide synthase. |journal=Genes Cells |volume=5 |issue= 11 |pages= 905-911 |year= 2001 |pmid= 11122378 |doi=  }}
* {{cite journal | vauthors = Bielli A, Thörnqvist PO, Hendrick AG, Finn R, Fitzgerald K, McCaffrey MW | title = The small GTPase Rab4A interacts with the central region of cytoplasmic dynein light intermediate chain-1 | journal = Biochemical and Biophysical Research Communications | volume = 281 | issue = 5 | pages = 1141–53 | date = Mar 2001 | pmid = 11243854 | doi = 10.1006/bbrc.2001.4468 }}
*{{cite journal | author=Lo KW, Naisbitt S, Fan JS, ''et al.'' |title=The 8-kDa dynein light chain binds to its targets via a conserved (K/R)XTQT motif. |journal=J. Biol. Chem. |volume=276 |issue= 17 |pages= 14059-66 |year= 2001 |pmid= 11148209 |doi= 10.1074/jbc.M010320200 }}
* {{cite journal | vauthors = Yu J, Yu L, Chen Z, Zheng L, Chen X, Wang X, Ren D, Zhao S | title = Protein inhibitor of neuronal nitric oxide synthase interacts with protein kinase A inhibitors | journal = Brain Research. Molecular Brain Research | volume = 99 | issue = 2 | pages = 145–9 | date = Mar 2002 | pmid = 11978406 | doi = 10.1016/S0169-328X(02)00104-3 }}
*{{cite journal | author=Yano H, Lee FS, Kong H, ''et al.'' |title=Association of Trk neurotrophin receptors with components of the cytoplasmic dynein motor. |journal=J. Neurosci. |volume=21 |issue= 3 |pages= RC125 |year= 2001 |pmid= 11157096 |doi= }}
* {{cite journal | vauthors = Fuhrmann JC, Kins S, Rostaing P, El Far O, Kirsch J, Sheng M, Triller A, Betz H, Kneussel M | title = Gephyrin interacts with Dynein light chains 1 and 2, components of motor protein complexes | journal = The Journal of Neuroscience | volume = 22 | issue = 13 | pages = 5393–402 | date = Jul 2002 | pmid = 12097491 }}
*{{cite journal | author=Fan J, Zhang Q, Tochio H, ''et al.'' |title=Structural basis of diverse sequence-dependent target recognition by the 8 kDa dynein light chain. |journal=J. Mol. Biol. |volume=306 |issue= 1 |pages= 97-108 |year= 2001 |pmid= 11178896 |doi= 10.1006/jmbi.2000.4374 }}
*{{cite journal | author=Bielli A, Thörnqvist PO, Hendrick AG, ''et al.'' |title=The small GTPase Rab4A interacts with the central region of cytoplasmic dynein light intermediate chain-1. |journal=Biochem. Biophys. Res. Commun. |volume=281 |issue= 5 |pages= 1141-53 |year= 2001 |pmid= 11243854 |doi= 10.1006/bbrc.2001.4468 }}
*{{cite journal  | author=Yu J, Yu L, Chen Z, ''et al.'' |title=Protein inhibitor of neuronal nitric oxide synthase interacts with protein kinase A inhibitors. |journal=Brain Res. Mol. Brain Res. |volume=99 |issue= 2 |pages= 145-9 |year= 2002 |pmid= 11978406 |doi=  }}
*{{cite journal  | author=Fuhrmann JC, Kins S, Rostaing P, ''et al.'' |title=Gephyrin interacts with Dynein light chains 1 and 2, components of motor protein complexes. |journal=J. Neurosci. |volume=22 |issue= 13 |pages= 5393-402 |year= 2002 |pmid= 12097491 |doi= 20026552 }}
}}
{{refend}}
{{refend}}
 
{{PDB Gallery|geneid=8655}}
{{protein-stub}}
{{WikiDoc Sources}}

Latest revision as of 18:47, 30 August 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Dynein light chain 1, cytoplasmic is a protein that in humans is encoded by the DYNLL1 gene.[1][2][3][4]

Function

Cytoplasmic dyneins are large enzyme complexes with a molecular mass of about 1,200 kD. They contain two force-producing heads formed primarily from dynein heavy chains, and stalks linking the heads to a basal domain, which contains a varying number of accessory intermediate chains. The complex is involved in intracellular transport and motility. The protein described in this record is a light chain and exists as part of this complex but also physically interacts with and inhibits the activity of neuronal nitric oxide synthase. Binding of this protein destabilizes the neuronal nitric oxide synthase dimer, a conformation necessary for activity, and it may regulate numerous biologic processes through its effects on nitric oxide synthase activity. Alternate transcriptional splice variants have been characterized.[4]

Interactions

DYNLL1 has been shown to interact with:

References

  1. ↑ Dick T, Ray K, Salz HK, Chia W (May 1996). "Cytoplasmic dynein (ddlc1) mutations cause morphogenetic defects and apoptotic cell death in Drosophila melanogaster". Molecular and Cellular Biology. 16 (5): 1966–77. doi:10.1128/mcb.16.5.1966. PMC 231184. PMID 8628263.
  2. ↑ Jaffrey SR, Snyder SH (Nov 1996). "PIN: an associated protein inhibitor of neuronal nitric oxide synthase". Science. 274 (5288): 774–7. doi:10.1126/science.274.5288.774. PMID 8864115.
  3. ↑ Pfister KK, Fisher EM, Gibbons IR, Hays TS, Holzbaur EL, McIntosh JR, Porter ME, Schroer TA, Vaughan KT, Witman GB, King SM, Vallee RB (Nov 2005). "Cytoplasmic dynein nomenclature". The Journal of Cell Biology. 171 (3): 411–3. doi:10.1083/jcb.200508078. PMC 2171247. PMID 16260502.
  4. ↑ 4.0 4.1 "Entrez Gene: DYNLL1 dynein, light chain, LC8-type 1".
  5. ↑ Day CL, Puthalakath H, Skea G, Strasser A, Barsukov I, Lian LY, Huang DC, Hinds MG (Feb 2004). "Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands". The Biochemical Journal. 377 (Pt 3): 597–605. doi:10.1042/BJ20031251. PMC 1223895. PMID 14561217.
  6. ↑ 6.0 6.1 Vadlamudi RK, Bagheri-Yarmand R, Yang Z, Balasenthil S, Nguyen D, Sahin AA, den Hollander P, Kumar R (Jun 2004). "Dynein light chain 1, a p21-activated kinase 1-interacting substrate, promotes cancerous phenotypes". Cancer Cell. 5 (6): 575–85. doi:10.1016/j.ccr.2004.05.022. PMID 15193260.
  7. ↑ 7.0 7.1 7.2 Naisbitt S, Valtschanoff J, Allison DW, Sala C, Kim E, Craig AM, Weinberg RJ, Sheng M (Jun 2000). "Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein". The Journal of Neuroscience. 20 (12): 4524–34. PMID 10844022.
  8. ↑ Diefenbach RJ, Diefenbach E, Douglas MW, Cunningham AL (Dec 2002). "The heavy chain of conventional kinesin interacts with the SNARE proteins SNAP25 and SNAP23". Biochemistry. 41 (50): 14906–15. doi:10.1021/bi026417u. PMID 12475239.
  9. ↑ Crépieux P, Kwon H, Leclerc N, Spencer W, Richard S, Lin R, Hiscott J (Dec 1997). "I kappaB alpha physically interacts with a cytoskeleton-associated protein through its signal response domain". Molecular and Cellular Biology. 17 (12): 7375–85. PMC 232593. PMID 9372968.
  10. ↑ Herzig RP, Andersson U, Scarpulla RC (Dec 2000). "Dynein light chain interacts with NRF-1 and EWG, structurally and functionally related transcription factors from humans and drosophila". Journal of Cell Science. 113 (23): 4263–73. PMID 11069771.
  11. ↑ Lo KW, Kan HM, Chan LN, Xu WG, Wang KP, Wu Z, Sheng M, Zhang M (Mar 2005). "The 8-kDa dynein light chain binds to p53-binding protein 1 and mediates DNA damage-induced p53 nuclear accumulation". The Journal of Biological Chemistry. 280 (9): 8172–9. doi:10.1074/jbc.M411408200. PMID 15611139.

Further reading

  • Robertson NG, Khetarpal U, Gutiérrez-Espeleta GA, Bieber FR, Morton CC (Sep 1994). "Isolation of novel and known genes from a human fetal cochlear cDNA library using subtractive hybridization and differential screening". Genomics. 23 (1): 42–50. doi:10.1006/geno.1994.1457. PMID 7829101.
  • Crépieux P, Kwon H, Leclerc N, Spencer W, Richard S, Lin R, Hiscott J (Dec 1997). "I kappaB alpha physically interacts with a cytoskeleton-associated protein through its signal response domain". Molecular and Cellular Biology. 17 (12): 7375–85. PMC 232593. PMID 9372968.
  • Tochio H, Ohki S, Zhang Q, Li M, Zhang M (Nov 1998). "Solution structure of a protein inhibitor of neuronal nitric oxide synthase". Nature Structural Biology. 5 (11): 965–9. doi:10.1038/2940. PMID 9808041.
  • Rodríguez-Crespo I, Straub W, Gavilanes F, Ortiz de Montellano PR (Nov 1998). "Binding of dynein light chain (PIN) to neuronal nitric oxide synthase in the absence of inhibition". Archives of Biochemistry and Biophysics. 359 (2): 297–304. doi:10.1006/abbi.1998.0928. PMID 9808772.
  • Fan JS, Zhang Q, Li M, Tochio H, Yamazaki T, Shimizu M, Zhang M (Dec 1998). "Protein inhibitor of neuronal nitric-oxide synthase, PIN, binds to a 17-amino acid residue fragment of the enzyme". The Journal of Biological Chemistry. 273 (50): 33472–81. doi:10.1074/jbc.273.50.33472. PMID 9837926.
  • Puthalakath H, Huang DC, O'Reilly LA, King SM, Strasser A (Mar 1999). "The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex". Molecular Cell. 3 (3): 287–96. doi:10.1016/S1097-2765(00)80456-6. PMID 10198631.
  • Liang J, Jaffrey SR, Guo W, Snyder SH, Clardy J (Aug 1999). "Structure of the PIN/LC8 dimer with a bound peptide". Nature Structural Biology. 6 (8): 735–40. doi:10.1038/11501. PMID 10426949.
  • Epstein E, Sela-Brown A, Ringel I, Kilav R, King SM, Benashski SE, Yisraeli JK, Silver J, Naveh-Many T (Feb 2000). "Dynein light chain binding to a 3'-untranslated sequence mediates parathyroid hormone mRNA association with microtubules". The Journal of Clinical Investigation. 105 (4): 505–12. doi:10.1172/JCI8557. PMC 289163. PMID 10683380.
  • Naisbitt S, Valtschanoff J, Allison DW, Sala C, Kim E, Craig AM, Weinberg RJ, Sheng M (Jun 2000). "Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein". The Journal of Neuroscience. 20 (12): 4524–34. PMID 10844022.
  • Jacob Y, Badrane H, Ceccaldi PE, Tordo N (Nov 2000). "Cytoplasmic dynein LC8 interacts with lyssavirus phosphoprotein". Journal of Virology. 74 (21): 10217–22. doi:10.1128/JVI.74.21.10217-10222.2000. PMC 102062. PMID 11024152.
  • Herzig RP, Andersson U, Scarpulla RC (Dec 2000). "Dynein light chain interacts with NRF-1 and EWG, structurally and functionally related transcription factors from humans and drosophila". Journal of Cell Science. 113 (23): 4263–73. PMID 11069771.
  • Haraguchi K, Satoh K, Yanai H, Hamada F, Kawabuchi M, Akiyama T (Nov 2000). "The hDLG-associated protein DAP interacts with dynein light chain and neuronal nitric oxide synthase". Genes to Cells. 5 (11): 905–911. doi:10.1046/j.1365-2443.2000.00374.x. PMID 11122378.
  • Lo KW, Naisbitt S, Fan JS, Sheng M, Zhang M (Apr 2001). "The 8-kDa dynein light chain binds to its targets via a conserved (K/R)XTQT motif". The Journal of Biological Chemistry. 276 (17): 14059–66. doi:10.1074/jbc.M010320200. PMID 11148209.
  • Yano H, Lee FS, Kong H, Chuang J, Arevalo J, Perez P, Sung C, Chao MV (Feb 2001). "Association of Trk neurotrophin receptors with components of the cytoplasmic dynein motor". The Journal of Neuroscience. 21 (3): RC125. PMID 11157096.
  • Fan J, Zhang Q, Tochio H, Li M, Zhang M (Feb 2001). "Structural basis of diverse sequence-dependent target recognition by the 8 kDa dynein light chain". Journal of Molecular Biology. 306 (1): 97–108. doi:10.1006/jmbi.2000.4374. PMID 11178896.
  • Bielli A, Thörnqvist PO, Hendrick AG, Finn R, Fitzgerald K, McCaffrey MW (Mar 2001). "The small GTPase Rab4A interacts with the central region of cytoplasmic dynein light intermediate chain-1". Biochemical and Biophysical Research Communications. 281 (5): 1141–53. doi:10.1006/bbrc.2001.4468. PMID 11243854.
  • Yu J, Yu L, Chen Z, Zheng L, Chen X, Wang X, Ren D, Zhao S (Mar 2002). "Protein inhibitor of neuronal nitric oxide synthase interacts with protein kinase A inhibitors". Brain Research. Molecular Brain Research. 99 (2): 145–9. doi:10.1016/S0169-328X(02)00104-3. PMID 11978406.
  • Fuhrmann JC, Kins S, Rostaing P, El Far O, Kirsch J, Sheng M, Triller A, Betz H, Kneussel M (Jul 2002). "Gephyrin interacts with Dynein light chains 1 and 2, components of motor protein complexes". The Journal of Neuroscience. 22 (13): 5393–402. PMID 12097491.
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