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2014 ; 5
(ä): e29513
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Formins as effector proteins of Rho GTPases
#MMPMID24914801
Kühn S
; Geyer M
Small GTPases
2014[]; 5
(ä): e29513
PMID24914801
show ga
Formin proteins were recognized as effectors of Rho GTPases some 15 years ago.
They contribute to different cellular actin cytoskeleton structures by their
ability to polymerize straight actin filaments at the barbed end. While not all
formins necessarily interact with Rho GTPases, a subgroup of mammalian formins,
termed Diaphanous-related formins or DRFs, were shown to be activated by small
GTPases of the Rho superfamily. DRFs are autoinhibited in the resting state by an
N- to C-terminal interaction that renders the central actin polymerization domain
inactive. Upon the interaction with a GTP-bound Rho, Rac, or Cdc42 GTPase, the
C-terminal autoregulation domain is displaced from its N-terminal recognition
site and the formin becomes active to polymerize actin filaments. In this review
we discuss the current knowledge on the structure, activation, and function of
formin-GTPase interactions for the mammalian formin families Dia, Daam, FMNL, and
FHOD. We describe both direct and indirect interactions of formins with GTPases,
which lead to formin activation and cytoskeletal rearrangements. The multifaceted
function of formins as effector proteins of Rho GTPases thus reflects the
diversity of the actin cytoskeleton in cells.
|Actin Cytoskeleton/metabolism
[MESH]
|Animals
[MESH]
|Binding Sites
[MESH]
|Carrier Proteins/chemistry/*metabolism
[MESH]
|Fetal Proteins/chemistry/*metabolism
[MESH]
|Formins
[MESH]
|Humans
[MESH]
|Intracellular Signaling Peptides and Proteins/chemistry/*metabolism
[MESH]
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