Abstract
Several new families of ARF GTPase activating proteins (ARF GAPs) have been described recently that associate with paxillin and other cytoskeletal and signaling proteins. Important insights have been gained regarding their subcellular distribution, enzymatic specificity and protein scaffold function. Evidence suggests an important role for ARF GAPs in mediating changes in the cell's actin cytoskeleton in response to adhesion and growth factor stimulation.
Publication types
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, P.H.S.
-
Review
MeSH terms
-
ADP-Ribosylation Factors / chemistry
-
ADP-Ribosylation Factors / physiology*
-
Actins / metabolism
-
Adaptor Proteins, Signal Transducing
-
Carrier Proteins / chemistry
-
Carrier Proteins / physiology
-
Cell Cycle Proteins*
-
Cytoskeletal Proteins / metabolism*
-
Cytoskeleton / metabolism*
-
GTPase-Activating Proteins / chemistry
-
GTPase-Activating Proteins / physiology*
-
Humans
-
Models, Biological
-
Paxillin
-
Phosphoproteins / metabolism*
-
Protein Structure, Tertiary
-
Signal Transduction
Substances
-
ARFGAP1 protein, human
-
ARFGAP3 protein, human
-
Actins
-
Adaptor Proteins, Signal Transducing
-
Carrier Proteins
-
Cell Cycle Proteins
-
Cytoskeletal Proteins
-
GIT1 protein, human
-
GTPase-Activating Proteins
-
PXN protein, human
-
Paxillin
-
Phosphoproteins
-
ASAP2 protein, human
-
ADP-Ribosylation Factors