MYO1A: Difference between revisions

Jump to navigation Jump to search
m (Robot: Automated text replacement (-{{WikiDoc Cardiology Network Infobox}} +, -<references /> +{{reflist|2}}, -{{reflist}} +{{reflist|2}}))
 
imported>InternetArchiveBot
(Rescuing 1 sources and tagging 0 as dead. #IABot (v1.6.1))
 
(One intermediate revision by one other user not shown)
Line 1: Line 1:
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Myosin-Ia''' is a [[protein]] that in humans is encoded by the ''MYO1A'' [[gene]].<ref name="pmid8884266">{{cite journal |vauthors=Hasson T, Skowron JF, Gilbert DJ, Avraham KB, Perry WL, Bement WM, Anderson BL, Sherr EH, Chen ZY, Greene LA, Ward DC, Corey DP, Mooseker MS, Copeland NG, Jenkins NA | title = Mapping of unconventional myosins in mouse and human | journal = Genomics | volume = 36 | issue = 3 | pages = 431–9 |date=Feb 1997 | pmid = 8884266 | pmc =  | doi = 10.1006/geno.1996.0488 }}</ref><ref name="pmid12736868">{{cite journal |vauthors=Donaudy F, Ferrara A, Esposito L, Hertzano R, Ben-David O, Bell RE, Melchionda S, Zelante L, Avraham KB, Gasparini P | title = Multiple mutations of MYO1A, a cochlear-expressed gene, in sensorineural hearing loss | journal = Am J Hum Genet | volume = 72 | issue = 6 | pages = 1571–7 |date=May 2003 | pmid = 12736868 | pmc = 1180318 | doi = 10.1086/375654 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: MYO1A myosin IA| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4640| 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. -->
The [[protein]] encoded by this gene belongs to the [[myosin]] superfamily. Myosins are molecular motors that, upon interaction with [[actin]] filaments, utilize energy from [[ATP hydrolysis]] to generate mechanical force. Each myosin has a conserved N-terminal motor domain that contains both ATP-binding and actin-binding sequences. Following the motor domain is a light-chain-binding 'neck' region containing 1-6 copies of a repeat element, the IQ motif, that serves as a binding site for [[calmodulin]] or other members of the [[EF hand|EF-hand]] superfamily of calcium-binding proteins. At the [[C-terminus]], each myosin class has a distinct tail domain that serves in dimerization, membrane binding, protein binding, and/or enzymatic activities and targets each myosin to its particular subcellular location. The myosin-1a protein is expressed by [[enterocytes]], the epithelial cells that line the luminal surface of the small intestine. In these cells the myosin-1a protein localizes specifically to the [[brush border]].  Experiments indicate that the brush border population of the encoded protein turns over rapidly, while its head and tail domains interact transiently with the core actin and plasma membrane, respectively. A rapidly exchanging pool of the myosin-1a protein binds to the actin core bundle, which turns over on a much slower timescale.<ref name="pmid11916846">{{cite journal | vauthors = Tyska MJ, Mooseker MS | title = MYO1A (brush border myosin I) dynamics in the brush border of LLC-PK1-CL4 cells | journal = Biophys. J. | volume = 82 | issue = 4 | pages = 1869–83 | date = April 2002 | pmid = 11916846 | pmc = 1301984 | url = http://www.biophysj.org/cgi/content/abstract/82/4/1869 | doi = 10.1016/S0006-3495(02)75537-9 | deadurl = yes | archiveurl = https://web.archive.org/web/20071227104735/http://www.biophysj.org/cgi/content/abstract/82/4/1869 | archivedate = 2007-12-27 | df = }}</ref>
{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Myosin IA
| HGNCid = 7595
| Symbol = MYO1A
| AltSymbols =; MIHC; BBMI; DFNA48; MYHL
| OMIM = 601478
| ECnumber = 
| Homologene = 21113
| MGIid = 107732
| GeneAtlas_image1 = PBB_GE_MYO1A_211916_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003774 |text = motor activity}} {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005516 |text = calmodulin binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}}
  | Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005902 |text = microvillus}} {{GNF_GO|id=GO:0005903 |text = brush border}} {{GNF_GO|id=GO:0016323 |text = basolateral plasma membrane}} {{GNF_GO|id=GO:0016328 |text = lateral plasma membrane}} {{GNF_GO|id=GO:0016459 |text = myosin complex}} {{GNF_GO|id=GO:0030864 |text = cortical actin cytoskeleton}} {{GNF_GO|id=GO:0031941 |text = filamentous actin}}
| Process = {{GNF_GO|id=GO:0007605 |text = sensory perception of sound}} {{GNF_GO|id=GO:0051648 |text = vesicle localization}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4640
    | Hs_Ensembl = ENSG00000166866
    | Hs_RefseqProtein = NP_005370
    | Hs_RefseqmRNA = NM_005379
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr = 12
    | Hs_GenLoc_start = 55708569
    | Hs_GenLoc_end = 55730160
    | Hs_Uniprot = Q9UBC5
    | Mm_EntrezGene = 432516
    | Mm_Ensembl = ENSMUSG00000025401
    | Mm_RefseqmRNA = XM_001005647
    | Mm_RefseqProtein = XP_001005647
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 10
    | Mm_GenLoc_start = 127108196
    | Mm_GenLoc_end = 127123884
    | Mm_Uniprot = 
  }}
}}
'''Myosin IA''', also known as '''Brush-border myosin-1''' and '''MYO1A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MYO1A myosin IA| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4640| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
==References==
{{PBB_Summary
{{reflist}}
| section_title =  
| summary_text = The protein encoded by this gene belongs to the myosin superfamily. Myosins are molecular motors that, upon interaction with actin filaments, utilize energy from ATP hydrolysis to generate mechanical force. Each myosin has a conserved N-terminal motor domain that contains both ATP-binding and actin-binding sequences. Following the motor domain is a light-chain-binding 'neck' region containing 1-6 copies of a repeat element, the IQ motif, that serves as a binding site for calmodulin or other members of the EF-hand superfamily of calcium-binding proteins. At the C-terminus, each myosin class has a distinct tail domain that serves in dimerization, membrane binding, protein binding, and/or enzymatic activities and targets each myosin to its particular subcellular location. The kidney epithelial cell line, LLC-PK1-CL4 (CL4), forms a well ordered brush border (BB) on its apical surface. Experiments indicate that the brush border population of the encoded protein turns over rapidly, while its head and tail domains interact transiently with the core actin and plasma membrane, respectively. A rapidly exchanging pool of the protein encoded by this gene envelops an actin core bundle that, by comparison, is static in structure.<ref name="entrez">{{cite web | title = Entrez Gene: MYO1A myosin IA| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4640| accessdate = }}</ref>
}}


==References==
{{reflist|2}}
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal | author=Hofmann WA, Johnson T, Klapczynski M, ''et al.'' |title=From transcription to transport: emerging roles for nuclear myosin I. |journal=Biochem. Cell Biol. |volume=84 |issue= 4 |pages= 418-26 |year= 2007 |pmid= 16936815 |doi= 10.1139/o06-069 }}
*{{cite journal   |vauthors=Hofmann WA, Johnson T, Klapczynski M, etal |title=From transcription to transport: emerging roles for nuclear myosin I. |journal=Biochem. Cell Biol. |volume=84 |issue= 4 |pages= 418–26 |year= 2007 |pmid= 16936815 |doi= 10.1139/o06-069 }}
*{{cite journal | author=Hoshimaru M, Fujio Y, Sobue K, ''et al.'' |title=Immunochemical evidence that myosin I heavy chain-like protein is identical to the 110-kilodalton brush-border protein. |journal=J. Biochem. |volume=106 |issue= 3 |pages= 455-9 |year= 1990 |pmid= 2606897 |doi=  }}
*{{cite journal   |vauthors=Hoshimaru M, Fujio Y, Sobue K, etal |title=Immunochemical evidence that myosin I heavy chain-like protein is identical to the 110-kilodalton brush-border protein. |journal=J. Biochem. |volume=106 |issue= 3 |pages= 455–9 |year= 1990 |pmid= 2606897 |doi=  }}
*{{cite journal | author=Bement WM, Hasson T, Wirth JA, ''et al.'' |title=Identification and overlapping expression of multiple unconventional myosin genes in vertebrate cell types. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 14 |pages= 6549-53 |year= 1994 |pmid= 8022818 |doi=  }}
*{{cite journal   |vauthors=Bement WM, Hasson T, Wirth JA, etal |title=Identification and overlapping expression of multiple unconventional myosin genes in vertebrate cell types. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 14 |pages= 6549–53 |year= 1994 |pmid= 8022818 |doi=10.1073/pnas.91.14.6549  | pmc=44240 }}
*{{cite journal | author=Durrbach A, Collins K, Matsudaira P, ''et al.'' |title=Brush border myosin-I truncated in the motor domain impairs the distribution and the function of endocytic compartments in an hepatoma cell line. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 14 |pages= 7053-8 |year= 1996 |pmid= 8692943 |doi=  }}
*{{cite journal   |vauthors=Durrbach A, Collins K, Matsudaira P, etal |title=Brush border myosin-I truncated in the motor domain impairs the distribution and the function of endocytic compartments in an hepatoma cell line. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 14 |pages= 7053–8 |year= 1996 |pmid= 8692943 |doi=10.1073/pnas.93.14.7053  | pmc=38934  }}
*{{cite journal  | author=Hasson T, Skowron JF, Gilbert DJ, ''et al.'' |title=Mapping of unconventional myosins in mouse and human. |journal=Genomics |volume=36 |issue= 3 |pages= 431-9 |year= 1997 |pmid= 8884266 |doi= 10.1006/geno.1996.0488 }}
*{{cite journal  |vauthors=Skowron JF, Bement WM, Mooseker MS |title=Human brush border myosin-I and myosin-Ic expression in human intestine and Caco-2BBe cells. |journal=Cell Motil. Cytoskeleton |volume=41 |issue= 4 |pages= 308–24 |year= 1999 |pmid= 9858156 |doi= 10.1002/(SICI)1097-0169(1998)41:4<308::AID-CM4>3.0.CO;2-J }}
*{{cite journal  | author=Skowron JF, Bement WM, Mooseker MS |title=Human brush border myosin-I and myosin-Ic expression in human intestine and Caco-2BBe cells. |journal=Cell Motil. Cytoskeleton |volume=41 |issue= 4 |pages= 308-24 |year= 1999 |pmid= 9858156 |doi= 10.1002/(SICI)1097-0169(1998)41:4<308::AID-CM4>3.0.CO;2-J }}
*{{cite journal   |vauthors=Li W, Wang J, Coluccio LM, etal |title=Brush border myosin I (BBMI): a basally localized transcript in human jejunal enterocytes. |journal=J. Histochem. Cytochem. |volume=48 |issue= 1 |pages= 89–94 |year= 2000 |pmid= 10653589 |doi= 10.1177/002215540004800109 }}
*{{cite journal | author=Li W, Wang J, Coluccio LM, ''et al.'' |title=Brush border myosin I (BBMI): a basally localized transcript in human jejunal enterocytes. |journal=J. Histochem. Cytochem. |volume=48 |issue= 1 |pages= 89-94 |year= 2000 |pmid= 10653589 |doi= }}
*{{cite journal  |vauthors=Otterbein LR, Graceffa P, Dominguez R |title=The crystal structure of uncomplexed actin in the ADP state. |journal=Science |volume=293 |issue= 5530 |pages= 708–11 |year= 2001 |pmid= 11474115 |doi= 10.1126/science.1059700 }}
*{{cite journal  | author=Otterbein LR, Graceffa P, Dominguez R |title=The crystal structure of uncomplexed actin in the ADP state. |journal=Science |volume=293 |issue= 5530 |pages= 708-11 |year= 2001 |pmid= 11474115 |doi= 10.1126/science.1059700 }}
*{{cite journal  |vauthors=Tyska MJ, Mooseker MS |title=MYO1A (brush border myosin I) dynamics in the brush border of LLC-PK1-CL4 cells. |journal=Biophys. J. |volume=82 |issue= 4 |pages= 1869–83 |year= 2002 |pmid= 11916846 |doi=10.1016/S0006-3495(02)75537-9  | pmc=1301984 }}
*{{cite journal  | author=Tyska MJ, Mooseker MS |title=MYO1A (brush border myosin I) dynamics in the brush border of LLC-PK1-CL4 cells. |journal=Biophys. J. |volume=82 |issue= 4 |pages= 1869-83 |year= 2002 |pmid= 11916846 |doi=  }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal   |vauthors=D'Adamo P, Pinna M, Capobianco S, etal |title=A novel autosomal dominant non-syndromic deafness locus (DFNA48) maps to 12q13-q14 in a large Italian family. |journal=Hum. Genet. |volume=112 |issue= 3 |pages= 319–20 |year= 2003 |pmid= 12596055 |doi= 10.1007/s00439-002-0880-6 }}
*{{cite journal | author=D'Adamo P, Pinna M, Capobianco S, ''et al.'' |title=A novel autosomal dominant non-syndromic deafness locus (DFNA48) maps to 12q13-q14 in a large Italian family. |journal=Hum. Genet. |volume=112 |issue= 3 |pages= 319-20 |year= 2003 |pmid= 12596055 |doi= 10.1007/s00439-002-0880-6 }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
*{{cite journal | author=Donaudy F, Ferrara A, Esposito L, ''et al.'' |title=Multiple mutations of MYO1A, a cochlear-expressed gene, in sensorineural hearing loss. |journal=Am. J. Hum. Genet. |volume=72 |issue= 6 |pages= 1571-7 |year= 2003 |pmid= 12736868 |doi=  }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
}}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{Cytoskeletal Proteins}}
{{WikiDoc Sources}}
 
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = no
| update_citations = yes
}}
 
 
{{gene-12-stub}}

Latest revision as of 03:29, 11 January 2018

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

Myosin-Ia is a protein that in humans is encoded by the MYO1A gene.[1][2][3]

The protein encoded by this gene belongs to the myosin superfamily. Myosins are molecular motors that, upon interaction with actin filaments, utilize energy from ATP hydrolysis to generate mechanical force. Each myosin has a conserved N-terminal motor domain that contains both ATP-binding and actin-binding sequences. Following the motor domain is a light-chain-binding 'neck' region containing 1-6 copies of a repeat element, the IQ motif, that serves as a binding site for calmodulin or other members of the EF-hand superfamily of calcium-binding proteins. At the C-terminus, each myosin class has a distinct tail domain that serves in dimerization, membrane binding, protein binding, and/or enzymatic activities and targets each myosin to its particular subcellular location. The myosin-1a protein is expressed by enterocytes, the epithelial cells that line the luminal surface of the small intestine. In these cells the myosin-1a protein localizes specifically to the brush border. Experiments indicate that the brush border population of the encoded protein turns over rapidly, while its head and tail domains interact transiently with the core actin and plasma membrane, respectively. A rapidly exchanging pool of the myosin-1a protein binds to the actin core bundle, which turns over on a much slower timescale.[4]

References

  1. Hasson T, Skowron JF, Gilbert DJ, Avraham KB, Perry WL, Bement WM, Anderson BL, Sherr EH, Chen ZY, Greene LA, Ward DC, Corey DP, Mooseker MS, Copeland NG, Jenkins NA (Feb 1997). "Mapping of unconventional myosins in mouse and human". Genomics. 36 (3): 431–9. doi:10.1006/geno.1996.0488. PMID 8884266.
  2. Donaudy F, Ferrara A, Esposito L, Hertzano R, Ben-David O, Bell RE, Melchionda S, Zelante L, Avraham KB, Gasparini P (May 2003). "Multiple mutations of MYO1A, a cochlear-expressed gene, in sensorineural hearing loss". Am J Hum Genet. 72 (6): 1571–7. doi:10.1086/375654. PMC 1180318. PMID 12736868.
  3. "Entrez Gene: MYO1A myosin IA".
  4. Tyska MJ, Mooseker MS (April 2002). "MYO1A (brush border myosin I) dynamics in the brush border of LLC-PK1-CL4 cells". Biophys. J. 82 (4): 1869–83. doi:10.1016/S0006-3495(02)75537-9. PMC 1301984. PMID 11916846. Archived from the original on 2007-12-27.

Further reading