TY - JOUR
T1 - Capping protein
T2 - New insights into mechanism and regulation
AU - Wear, Martin A.
AU - Cooper, John A.
N1 - Funding Information:
We are grateful to members of the Cooper laboratory for helpful discussions and to the reviewers for insightful comments and suggestions. The writing of this review was supported by a grant (GM38542) from the National Institutes of Health to J.A.C.
PY - 2004/8
Y1 - 2004/8
N2 - Temporal and spatial control of the actin cytoskeleton are crucial for a range of eukaryotic cellular processes. Capping protein (CP), a ubiquitous highly conserved heterodimer, tightly caps the barbed (fast-growing) end of the actin filament and is an important component in the assembly of various actin structures, including the dynamic branched filament network at the leading edge of motile cells. New research into the molecular mechanism of how CP interacts with the actin filament in vitro and the function of CP in vivo, including discoveries of novel interactions of CP with other proteins, has greatly enhanced our understanding of the role of CP in regulating the actin cytoskeleton.
AB - Temporal and spatial control of the actin cytoskeleton are crucial for a range of eukaryotic cellular processes. Capping protein (CP), a ubiquitous highly conserved heterodimer, tightly caps the barbed (fast-growing) end of the actin filament and is an important component in the assembly of various actin structures, including the dynamic branched filament network at the leading edge of motile cells. New research into the molecular mechanism of how CP interacts with the actin filament in vitro and the function of CP in vivo, including discoveries of novel interactions of CP with other proteins, has greatly enhanced our understanding of the role of CP in regulating the actin cytoskeleton.
UR - http://www.scopus.com/inward/record.url?scp=4043147895&partnerID=8YFLogxK
U2 - 10.1016/j.tibs.2004.06.003
DO - 10.1016/j.tibs.2004.06.003
M3 - Review article
C2 - 15362226
AN - SCOPUS:4043147895
SN - 0968-0004
VL - 29
SP - 418
EP - 428
JO - Trends in biochemical sciences
JF - Trends in biochemical sciences
IS - 8
ER -