The paxillin LD motifs
The paxillin LD motifs
Adapter/scaffold proteins, through their multidomain structure, perform a fundamental role in facilitating signal transduction within cells. Paxillin is a focal adhesion adapter protein implicated in growth factor- as well as integrin-mediated signaling pathways. The amino-terminus of paxillin contains five leucine-rich sequences termed LD motifs. These paxillin LD motifs are highly conserved between species as well as within the paxillin superfamily. They mediate interactions with several structural and regulatory proteins important for coordinating changes in the actin cytoskeleton associated with cell motility and cell adhesion as well as in the regulation of gene expression
actin cytoskeleton, cell adhesion, focal adhesion, integrin signaling
114-118
Tumbarello, David A.
75c6932e-fdbf-4d3c-bb4f-48fbbdba93a2
Brown, Michael C.
3f7046eb-5b0e-4813-8537-a8e1b09c611e
Turner, Christopher E.
a6c1a6bf-91ae-4d92-9980-0534fb696850
February 2002
Tumbarello, David A.
75c6932e-fdbf-4d3c-bb4f-48fbbdba93a2
Brown, Michael C.
3f7046eb-5b0e-4813-8537-a8e1b09c611e
Turner, Christopher E.
a6c1a6bf-91ae-4d92-9980-0534fb696850
Abstract
Adapter/scaffold proteins, through their multidomain structure, perform a fundamental role in facilitating signal transduction within cells. Paxillin is a focal adhesion adapter protein implicated in growth factor- as well as integrin-mediated signaling pathways. The amino-terminus of paxillin contains five leucine-rich sequences termed LD motifs. These paxillin LD motifs are highly conserved between species as well as within the paxillin superfamily. They mediate interactions with several structural and regulatory proteins important for coordinating changes in the actin cytoskeleton associated with cell motility and cell adhesion as well as in the regulation of gene expression
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Published date: February 2002
Keywords:
actin cytoskeleton, cell adhesion, focal adhesion, integrin signaling
Organisations:
Centre for Biological Sciences
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Local EPrints ID: 362406
URI: http://eprints.soton.ac.uk/id/eprint/362406
ISSN: 0014-5793
PURE UUID: 0ce9f3f6-3e97-4294-89c8-96517ae436e4
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Date deposited: 22 Aug 2014 10:17
Last modified: 15 Mar 2024 03:50
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Author:
Michael C. Brown
Author:
Christopher E. Turner
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