TRIM15 is a focal adhesion protein that regulates focal adhesion disassembly

Pradeep D. Uchil; Tobias Pawliczek; Tracy D. Reynolds; Siyuan Ding; Angelika Hinz; James B. Munro; Fang Huang; Robert W. Floyd; Haitao Yang; William L. Hamilton; Joerg Bewersdorf; Yong Xiong; David A. Calderwood; Walther Mothes

doi:10.1242/jcs.143537

TRIM15 is a focal adhesion protein that regulates focal adhesion disassembly

Pradeep D. Uchil, Tobias Pawliczek, Tracy D. Reynolds, Siyuan Ding, Angelika Hinz, James B. Munro, Fang Huang, Robert W. Floyd, Haitao Yang, William L. Hamilton, Joerg Bewersdorf, Yong Xiong, David A. Calderwood, Walther Mothes

Research output: Contribution to journal › Article › peer-review

21 Scopus citations

Abstract

Focal adhesions are macromolecular complexes that connect the actin cytoskeleton to the extracellular matrix. Dynamic turnover of focal adhesions is crucial for cell migration. Paxillin is a multiadaptor protein that plays an important role in regulating focal adhesion dynamics. Here, we identify TRIM15, a member of the tripartite motif protein family, as a paxillin-interacting factor and a component of focal adhesions. TRIM15 localizes to focal contacts in a myosin-II-independent manner by an interaction between its coiled-coil domain and the LD2 motif of paxillin. Unlike other focal adhesion proteins, TRIM15 is a stable focal adhesion component with restricted mobility due to its ability to form oligomers. TRIM15- depleted cells display impaired cell migration and reduced focal adhesion disassembly rates, in addition to enlarged focal adhesions. Thus, our studies demonstrate a cellular function for TRIM15 as a regulatory component of focal adhesion turnover and cell migration.

Original language	English
Pages (from-to)	3928-3942
Number of pages	15
Journal	Journal of cell science
Volume	127
Issue number	18
DOIs	https://doi.org/10.1242/jcs.143537
State	Published - 2014

Keywords

Cell migration
Focal adhesion disassembly
Focal adhesions
Paxillin
TRIM E3 ligases
TRIM15

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title = "TRIM15 is a focal adhesion protein that regulates focal adhesion disassembly",

abstract = "Focal adhesions are macromolecular complexes that connect the actin cytoskeleton to the extracellular matrix. Dynamic turnover of focal adhesions is crucial for cell migration. Paxillin is a multiadaptor protein that plays an important role in regulating focal adhesion dynamics. Here, we identify TRIM15, a member of the tripartite motif protein family, as a paxillin-interacting factor and a component of focal adhesions. TRIM15 localizes to focal contacts in a myosin-II-independent manner by an interaction between its coiled-coil domain and the LD2 motif of paxillin. Unlike other focal adhesion proteins, TRIM15 is a stable focal adhesion component with restricted mobility due to its ability to form oligomers. TRIM15- depleted cells display impaired cell migration and reduced focal adhesion disassembly rates, in addition to enlarged focal adhesions. Thus, our studies demonstrate a cellular function for TRIM15 as a regulatory component of focal adhesion turnover and cell migration.",

keywords = "Cell migration, Focal adhesion disassembly, Focal adhesions, Paxillin, TRIM E3 ligases, TRIM15",

author = "Uchil, {Pradeep D.} and Tobias Pawliczek and Reynolds, {Tracy D.} and Siyuan Ding and Angelika Hinz and Munro, {James B.} and Fang Huang and Floyd, {Robert W.} and Haitao Yang and Hamilton, {William L.} and Joerg Bewersdorf and Yong Xiong and Calderwood, {David A.} and Walther Mothes",

note = "Publisher Copyright: {\textcopyright} 2014. Published by The Company of Biologists Ltd.",

year = "2014",

doi = "10.1242/jcs.143537",

language = "English",

volume = "127",

pages = "3928--3942",

journal = "Journal of cell science",

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T1 - TRIM15 is a focal adhesion protein that regulates focal adhesion disassembly

AU - Uchil, Pradeep D.

AU - Pawliczek, Tobias

AU - Reynolds, Tracy D.

AU - Ding, Siyuan

AU - Hinz, Angelika

AU - Munro, James B.

AU - Huang, Fang

AU - Floyd, Robert W.

AU - Yang, Haitao

AU - Hamilton, William L.

AU - Bewersdorf, Joerg

AU - Xiong, Yong

AU - Calderwood, David A.

AU - Mothes, Walther

PY - 2014

Y1 - 2014

N2 - Focal adhesions are macromolecular complexes that connect the actin cytoskeleton to the extracellular matrix. Dynamic turnover of focal adhesions is crucial for cell migration. Paxillin is a multiadaptor protein that plays an important role in regulating focal adhesion dynamics. Here, we identify TRIM15, a member of the tripartite motif protein family, as a paxillin-interacting factor and a component of focal adhesions. TRIM15 localizes to focal contacts in a myosin-II-independent manner by an interaction between its coiled-coil domain and the LD2 motif of paxillin. Unlike other focal adhesion proteins, TRIM15 is a stable focal adhesion component with restricted mobility due to its ability to form oligomers. TRIM15- depleted cells display impaired cell migration and reduced focal adhesion disassembly rates, in addition to enlarged focal adhesions. Thus, our studies demonstrate a cellular function for TRIM15 as a regulatory component of focal adhesion turnover and cell migration.

AB - Focal adhesions are macromolecular complexes that connect the actin cytoskeleton to the extracellular matrix. Dynamic turnover of focal adhesions is crucial for cell migration. Paxillin is a multiadaptor protein that plays an important role in regulating focal adhesion dynamics. Here, we identify TRIM15, a member of the tripartite motif protein family, as a paxillin-interacting factor and a component of focal adhesions. TRIM15 localizes to focal contacts in a myosin-II-independent manner by an interaction between its coiled-coil domain and the LD2 motif of paxillin. Unlike other focal adhesion proteins, TRIM15 is a stable focal adhesion component with restricted mobility due to its ability to form oligomers. TRIM15- depleted cells display impaired cell migration and reduced focal adhesion disassembly rates, in addition to enlarged focal adhesions. Thus, our studies demonstrate a cellular function for TRIM15 as a regulatory component of focal adhesion turnover and cell migration.

KW - Cell migration

KW - Focal adhesion disassembly

KW - Focal adhesions

KW - Paxillin

KW - TRIM E3 ligases

KW - TRIM15

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U2 - 10.1242/jcs.143537

DO - 10.1242/jcs.143537

M3 - Article

C2 - 25015296

AN - SCOPUS:84907055711

SN - 0021-9533

VL - 127

SP - 3928

EP - 3942

JO - Journal of cell science

JF - Journal of cell science

IS - 18

ER -

TRIM15 is a focal adhesion protein that regulates focal adhesion disassembly

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