ARPC2: 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>CV9933
(CS1 maint - template details.)
 
(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
'''Actin-related protein 2/3 complex subunit 2''' is a [[protein]] that in humans is encoded by the ''ARPC2'' [[gene]].<ref name="pmid9359840">{{cite journal | vauthors = Machesky LM, Reeves E, Wientjes F, Mattheyse FJ, Grogan A, Totty NF, Burlingame AL, Hsuan JJ, Segal AW | title = Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionarily conserved proteins | journal = Biochem. J. | volume = 328 ( Pt 1) | issue = Pt 1 | pages = 105–12 | year = 1997 | pmid = 9359840 | pmc = 1218893 | doi =  }}</ref><ref name="pmid9230079">{{cite journal | vauthors = Welch MD, DePace AH, Verma S, Iwamatsu A, Mitchison TJ | title = The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filament assembly | journal = J. Cell Biol. | volume = 138 | issue = 2 | pages = 375–84  | date = August 1997 | pmid = 9230079 | pmc = 2138188 | doi = 10.1083/jcb.138.2.375 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ARPC2 actin related protein 2/3 complex, subunit 2, 34kDa| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10109| 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_ARPC2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1k8k.
| PDB = {{PDB2|1k8k}}, {{PDB2|1tyq}}, {{PDB2|1u2v}}, {{PDB2|2p9i}}, {{PDB2|2p9k}}, {{PDB2|2p9l}}, {{PDB2|2p9n}}, {{PDB2|2p9p}}, {{PDB2|2p9s}}, {{PDB2|2p9u}}
| Name = Actin related protein 2/3 complex, subunit 2, 34kDa
| HGNCid = 705
| Symbol = ARPC2
| AltSymbols =; ARC34; PNAS-139; PRO2446; p34-Arc
| OMIM = 604224
| ECnumber = 
| Homologene = 4187
| MGIid = 1923959
| GeneAtlas_image1 = PBB_GE_ARPC2_207988_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ARPC2_208679_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_ARPC2_213513_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005200 |text = structural constituent of cytoskeleton}}
| Component = {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0005885 |text = Arp2/3 protein complex}} {{GNF_GO|id=GO:0005925 |text = focal adhesion}}
| Process = {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0030833 |text = regulation of actin filament polymerization}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 10109
    | Hs_Ensembl = ENSG00000163466
    | Hs_RefseqProtein = NP_005722
    | Hs_RefseqmRNA = NM_005731
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 218790119
    | Hs_GenLoc_end = 218827315
    | Hs_Uniprot = O15144
    | Mm_EntrezGene = 76709
    | Mm_Ensembl = ENSMUSG00000006304
    | Mm_RefseqmRNA = XM_001000077
    | Mm_RefseqProtein = XP_001000077
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 1
    | Mm_GenLoc_start = 74169784
    | Mm_GenLoc_end = 74197664
    | Mm_Uniprot = Q3UA52
  }}
}}
'''Actin related protein 2/3 complex, subunit 2, 34kDa''', also known as '''ARPC2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ARPC2 actin related protein 2/3 complex, subunit 2, 34kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10109| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
This gene encodes one of seven subunits of the human Arp2/3 protein complex. The Arp2/3 protein complex has been implicated in the control of actin polymerization in cells and has been conserved through evolution. The exact role of the protein encoded by this gene, the p34 subunit, has yet to be determined. Two alternatively spliced variants have been characterized to date. Additional alternatively spliced variants have been described but their full length nature has not been determined.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = This gene encodes one of seven subunits of the human Arp2/3 protein complex. The Arp2/3 protein complex has been implicated in the control of actin polymerization in cells and has been conserved through evolution. The exact role of the protein encoded by this gene, the p34 subunit, has yet to be determined. Two alternatively spliced variants have been characterized to date. Additional alternatively spliced variants have been described but their full length nature has not been determined.<ref name="entrez">{{cite web | title = Entrez Gene: ARPC2 actin related protein 2/3 complex, subunit 2, 34kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10109| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
ARPC2 has been shown to [[Protein-protein interaction|interact]] with [[Cortactin]].<ref name=pmid11018051>{{cite journal | vauthors = Weed SA, Karginov AV, Schafer DA, Weaver AM, Kinley AW, Cooper JA, Parsons JT | title = Cortactin localization to sites of actin assembly in lamellipodia requires interactions with F-actin and the Arp2/3 complex | journal = J. Cell Biol. | volume = 151 | issue = 1 | pages = 29–40  | date = October 2000 | pmid = 11018051 | pmc = 2189811 | doi = 10.1083/jcb.151.1.29 }}</ref>
 
== References ==
{{reflist}}
 
==External links==
* {{UCSC gene info|ARPC2}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Couch FJ, Rommens JM, Neuhausen SL, Bélanger C, Dumont M, Abel K, Bell R, Berry S, Bogden R, Cannon-Albright L, Farid L, Frye C, Hattier T, Janecki T, Jiang P, Kehrer R, Leblanc JF, McArthur-Morrison J, Meney D, Miki Y, Peng Y, Samson C, Schroeder M, Snyder SC, Simard J | title = Generation of an integrated transcription map of the BRCA2 region on chromosome 13q12-q13 | journal = Genomics | volume = 36 | issue = 1 | pages = 86–99 | year = 1996 | pmid = 8812419 | doi = 10.1006/geno.1996.0428 }}
| citations =
* {{cite journal | vauthors = Welch MD, Iwamatsu A, Mitchison TJ | title = Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes | journal = Nature | volume = 385 | issue = 6613 | pages = 265–9 | year = 1997 | pmid = 9000076 | doi = 10.1038/385265a0 }}
*{{cite journal | author=Couch FJ, Rommens JM, Neuhausen SL, ''et al.'' |title=Generation of an integrated transcription map of the BRCA2 region on chromosome 13q12-q13. |journal=Genomics |volume=36 |issue= 1 |pages= 86-99 |year= 1997 |pmid= 8812419 |doi= }}
* {{cite journal | vauthors = Näär AM, Beaurang PA, Zhou S, Abraham S, Solomon W, Tjian R | title = Composite co-activator ARC mediates chromatin-directed transcriptional activation | journal = Nature | volume = 398 | issue = 6730 | pages = 828–32 | year = 1999 | pmid = 10235267 | doi = 10.1038/19789 }}
*{{cite journal | author=Welch MD, Iwamatsu A, Mitchison TJ |title=Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes. |journal=Nature |volume=385 |issue= 6613 |pages= 265-9 |year= 1997 |pmid= 9000076 |doi= 10.1038/385265a0 }}
* {{cite journal | vauthors = Zhao X, Yang Z, Qian M, Zhu X | title = Interactions among subunits of human Arp2/3 complex: p20-Arc as the hub | journal = Biochem. Biophys. Res. Commun. | volume = 280 | issue = 2 | pages = 513–7 | year = 2001 | pmid = 11162547 | doi = 10.1006/bbrc.2000.4151 }}
*{{cite journal | author=Welch MD, DePace AH, Verma S, ''et al.'' |title=The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filament assembly. |journal=J. Cell Biol. |volume=138 |issue= 2 |pages= 375-84 |year= 1997 |pmid= 9230079 |doi=  }}
* {{cite journal | vauthors = Robinson RC, Turbedsky K, Kaiser DA, Marchand JB, Higgs HN, Choe S, Pollard TD | title = Crystal structure of Arp2/3 complex | journal = Science | volume = 294 | issue = 5547 | pages = 1679–84 | year = 2001 | pmid = 11721045 | doi = 10.1126/science.1066333 }}
*{{cite journal  | author=Machesky LM, Reeves E, Wientjes F, ''et al.'' |title=Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionarily conserved proteins. |journal=Biochem. J. |volume=328 ( Pt 1) |issue=  |pages= 105-12 |year= 1998 |pmid= 9359840 |doi=  }}
* {{cite journal | vauthors = Gournier H, Goley ED, Niederstrasser H, Trinh T, Welch MD | title = Reconstitution of human Arp2/3 complex reveals critical roles of individual subunits in complex structure and activity | journal = Mol. Cell | volume = 8 | issue = 5 | pages = 1041–52 | year = 2001 | pmid = 11741539 | doi = 10.1016/S1097-2765(01)00393-8 }}
*{{cite journal  | author=Näär AM, Beaurang PA, Zhou S, ''et al.'' |title=Composite co-activator ARC mediates chromatin-directed transcriptional activation. |journal=Nature |volume=398 |issue= 6730 |pages= 828-32 |year= 1999 |pmid= 10235267 |doi= 10.1038/19789 }}
* {{cite journal | vauthors = Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J | title = Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides | journal = Nat. Biotechnol. | volume = 21 | issue = 5 | pages = 566–9 | year = 2003 | pmid = 12665801 | doi = 10.1038/nbt810 }}
*{{cite journal | author=Zhao X, Yang Z, Qian M, Zhu X |title=Interactions among subunits of human Arp2/3 complex: p20-Arc as the hub. |journal=Biochem. Biophys. Res. Commun. |volume=280 |issue= 2 |pages= 513-7 |year= 2001 |pmid= 11162547 |doi= 10.1006/bbrc.2000.4151 }}
* {{cite journal | vauthors = Kaneda A, Kaminishi M, Sugimura T, Ushijima T | title = Decreased expression of the seven ARP2/3 complex genes in human gastric cancers | journal = Cancer Lett. | volume = 212 | issue = 2 | pages = 203–10 | year = 2004 | pmid = 15279900 | doi = 10.1016/j.canlet.2004.03.020 }}
*{{cite journal | author=Robinson RC, Turbedsky K, Kaiser DA, ''et al.'' |title=Crystal structure of Arp2/3 complex. |journal=Science |volume=294 |issue= 5547 |pages= 1679-84 |year= 2001 |pmid= 11721045 |doi= 10.1126/science.1066333 }}
* {{cite journal | vauthors = Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, Mann M | title = Nucleolar proteome dynamics | journal = Nature | volume = 433 | issue = 7021 | pages = 77–83 | year = 2005 | pmid = 15635413 | doi = 10.1038/nature03207 }}
*{{cite journal | author=Gournier H, Goley ED, Niederstrasser H, ''et al.'' |title=Reconstitution of human Arp2/3 complex reveals critical roles of individual subunits in complex structure and activity. |journal=Mol. Cell |volume=8 |issue= 5 |pages= 1041-52 |year= 2002 |pmid= 11741539 |doi= }}
* {{cite journal | vauthors = Dubois T, Paléotti O, Mironov AA, Fraisier V, Stradal TE, De Matteis MA, Franco M, Chavrier P | title = Golgi-localized GAP for Cdc42 functions downstream of ARF1 to control Arp2/3 complex and F-actin dynamics | journal = Nat. Cell Biol. | volume = 7 | issue = 4 | pages = 353–64 | year = 2005 | pmid = 15793564 | doi = 10.1038/ncb1244 }}
*{{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 = Cai L, Holoweckyj N, Schaller MD, Bear JE | title = Phosphorylation of coronin 1B by protein kinase C regulates interaction with Arp2/3 and cell motility | journal = J. Biol. Chem. | volume = 280 | issue = 36 | pages = 31913–23 | year = 2005 | pmid = 16027158 | doi = 10.1074/jbc.M504146200 }}
*{{cite journal | author=Gevaert K, Goethals M, Martens L, ''et al.'' |title=Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. |journal=Nat. Biotechnol. |volume=21 |issue= 5 |pages= 566-9 |year= 2004 |pmid= 12665801 |doi= 10.1038/nbt810 }}
* {{cite journal | vauthors = Cai L, Marshall TW, Uetrecht AC, Schafer DA, Bear JE | title = Coronin 1B coordinates Arp2/3 complex and cofilin activities at the leading edge | journal = Cell | volume = 128 | issue = 5 | pages = 915–29 | year = 2007 | pmid = 17350576 | pmc = 2630706 | doi = 10.1016/j.cell.2007.01.031 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
* {{cite journal | vauthors = Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D | title = Large-scale mapping of human protein-protein interactions by mass spectrometry | journal = Mol. Syst. Biol. | volume = 3 | issue = 1 | pages = 89 | year = 2007 | pmid = 17353931 | pmc = 1847948 | doi = 10.1038/msb4100134 }}
*{{cite journal  | author=Kaneda A, Kaminishi M, Sugimura T, Ushijima T |title=Decreased expression of the seven ARP2/3 complex genes in human gastric cancers. |journal=Cancer Lett. |volume=212 |issue= 2 |pages= 203-10 |year= 2004 |pmid= 15279900 |doi= 10.1016/j.canlet.2004.03.020 }}
*{{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 }}
*{{cite journal  | author=Andersen JS, Lam YW, Leung AK, ''et al.'' |title=Nucleolar proteome dynamics. |journal=Nature |volume=433 |issue= 7021 |pages= 77-83 |year= 2005 |pmid= 15635413 |doi= 10.1038/nature03207 }}
*{{cite journal | author=Dubois T, Paléotti O, Mironov AA, ''et al.'' |title=Golgi-localized GAP for Cdc42 functions downstream of ARF1 to control Arp2/3 complex and F-actin dynamics. |journal=Nat. Cell Biol. |volume=7 |issue= 4 |pages= 353-64 |year= 2005 |pmid= 15793564 |doi= 10.1038/ncb1244 }}
*{{cite journal | author=Cai L, Holoweckyj N, Schaller MD, Bear JE |title=Phosphorylation of coronin 1B by protein kinase C regulates interaction with Arp2/3 and cell motility. |journal=J. Biol. Chem. |volume=280 |issue= 36 |pages= 31913-23 |year= 2005 |pmid= 16027158 |doi= 10.1074/jbc.M504146200 }}
*{{cite journal | author=Cai L, Marshall TW, Uetrecht AC, ''et al.'' |title=Coronin 1B coordinates Arp2/3 complex and cofilin activities at the leading edge. |journal=Cell |volume=128 |issue= 5 |pages= 915-29 |year= 2007 |pmid= 17350576 |doi= 10.1016/j.cell.2007.01.031 }}
*{{cite journal | author=Ewing RM, Chu P, Elisma F, ''et al.'' |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue= |pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
== External links ==
{{WikiDoc Sources}}
* {{UCSC genome browser|ARPC2}}
* {{UCSC gene details|ARPC2}}
 
{{PDB Gallery|geneid=10109}}
 
 
{{gene-2-stub}}

Latest revision as of 15:13, 26 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

Actin-related protein 2/3 complex subunit 2 is a protein that in humans is encoded by the ARPC2 gene.[1][2][3]

Function

This gene encodes one of seven subunits of the human Arp2/3 protein complex. The Arp2/3 protein complex has been implicated in the control of actin polymerization in cells and has been conserved through evolution. The exact role of the protein encoded by this gene, the p34 subunit, has yet to be determined. Two alternatively spliced variants have been characterized to date. Additional alternatively spliced variants have been described but their full length nature has not been determined.[3]

Interactions

ARPC2 has been shown to interact with Cortactin.[4]

References

  1. Machesky LM, Reeves E, Wientjes F, Mattheyse FJ, Grogan A, Totty NF, Burlingame AL, Hsuan JJ, Segal AW (1997). "Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionarily conserved proteins". Biochem. J. 328 ( Pt 1) (Pt 1): 105–12. PMC 1218893. PMID 9359840.
  2. Welch MD, DePace AH, Verma S, Iwamatsu A, Mitchison TJ (August 1997). "The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filament assembly". J. Cell Biol. 138 (2): 375–84. doi:10.1083/jcb.138.2.375. PMC 2138188. PMID 9230079.
  3. 3.0 3.1 "Entrez Gene: ARPC2 actin related protein 2/3 complex, subunit 2, 34kDa".
  4. Weed SA, Karginov AV, Schafer DA, Weaver AM, Kinley AW, Cooper JA, Parsons JT (October 2000). "Cortactin localization to sites of actin assembly in lamellipodia requires interactions with F-actin and the Arp2/3 complex". J. Cell Biol. 151 (1): 29–40. doi:10.1083/jcb.151.1.29. PMC 2189811. PMID 11018051.

External links

Further reading

  • Couch FJ, Rommens JM, Neuhausen SL, Bélanger C, Dumont M, Abel K, Bell R, Berry S, Bogden R, Cannon-Albright L, Farid L, Frye C, Hattier T, Janecki T, Jiang P, Kehrer R, Leblanc JF, McArthur-Morrison J, Meney D, Miki Y, Peng Y, Samson C, Schroeder M, Snyder SC, Simard J (1996). "Generation of an integrated transcription map of the BRCA2 region on chromosome 13q12-q13". Genomics. 36 (1): 86–99. doi:10.1006/geno.1996.0428. PMID 8812419.
  • Welch MD, Iwamatsu A, Mitchison TJ (1997). "Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes". Nature. 385 (6613): 265–9. doi:10.1038/385265a0. PMID 9000076.
  • Näär AM, Beaurang PA, Zhou S, Abraham S, Solomon W, Tjian R (1999). "Composite co-activator ARC mediates chromatin-directed transcriptional activation". Nature. 398 (6730): 828–32. doi:10.1038/19789. PMID 10235267.
  • Zhao X, Yang Z, Qian M, Zhu X (2001). "Interactions among subunits of human Arp2/3 complex: p20-Arc as the hub". Biochem. Biophys. Res. Commun. 280 (2): 513–7. doi:10.1006/bbrc.2000.4151. PMID 11162547.
  • Robinson RC, Turbedsky K, Kaiser DA, Marchand JB, Higgs HN, Choe S, Pollard TD (2001). "Crystal structure of Arp2/3 complex". Science. 294 (5547): 1679–84. doi:10.1126/science.1066333. PMID 11721045.
  • Gournier H, Goley ED, Niederstrasser H, Trinh T, Welch MD (2001). "Reconstitution of human Arp2/3 complex reveals critical roles of individual subunits in complex structure and activity". Mol. Cell. 8 (5): 1041–52. doi:10.1016/S1097-2765(01)00393-8. PMID 11741539.
  • Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (2003). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
  • Kaneda A, Kaminishi M, Sugimura T, Ushijima T (2004). "Decreased expression of the seven ARP2/3 complex genes in human gastric cancers". Cancer Lett. 212 (2): 203–10. doi:10.1016/j.canlet.2004.03.020. PMID 15279900.
  • Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, Mann M (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
  • Dubois T, Paléotti O, Mironov AA, Fraisier V, Stradal TE, De Matteis MA, Franco M, Chavrier P (2005). "Golgi-localized GAP for Cdc42 functions downstream of ARF1 to control Arp2/3 complex and F-actin dynamics". Nat. Cell Biol. 7 (4): 353–64. doi:10.1038/ncb1244. PMID 15793564.
  • Cai L, Holoweckyj N, Schaller MD, Bear JE (2005). "Phosphorylation of coronin 1B by protein kinase C regulates interaction with Arp2/3 and cell motility". J. Biol. Chem. 280 (36): 31913–23. doi:10.1074/jbc.M504146200. PMID 16027158.
  • Cai L, Marshall TW, Uetrecht AC, Schafer DA, Bear JE (2007). "Coronin 1B coordinates Arp2/3 complex and cofilin activities at the leading edge". Cell. 128 (5): 915–29. doi:10.1016/j.cell.2007.01.031. PMC 2630706. PMID 17350576.
  • Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

External links