Rho GTPases are molecular switches that regulate many essential cellular
processes, including actin dynamics, gene transcription, cell-cycle
progression and cell adhesion. In the GTP-bound form they are able to interact
with effector or target molecules to initiate a downstream response, while an
intrinsic GTPase activity returns the proteins to the GDP-bound state, to
complete the cycle and terminate signal transduction. The Rho effector motif
class 1 (REM-1) domain specifically binds GTP-Rho and is widely conserved in
the following Rho effector proteins [1,2,3]:
Vertebrate serine/threonine-protein kinases N (PKNs), contain three copies
of the REM-1 domain. Many proteins that interact with PKNs are involved
with the cytoskeletal network, e.g. α-actinin and vimentin. PKNs are
also implicated in the control of transcrption factors, mitogenesis, and
cell regulation. PKNs have also been shown to play a role in apoptosis and
to be involved in keratinocyte cell-cell adhesion with increased PKN
activity promoting cell-cell adhesion [4,5].
Animal transducer of Cdc42-dependent actin assembly (TOCA) family proteins,
comprise an N-terminal F-BAR domain (see <PDOC51741>), a central REM-1
domain, and a C-terminal SH3 domain (see <PDOC50002>) .
Yeast protein kinase C-like 1 (PKC1).
The REM-1 domain contains two long α helices forming a left-handed
antiparallel coiled-coil fold (see <PDB:5FRG>) termed the antiparallel coiled-coil (ACC) finger domain. The two long helices encompass the basic region and
the leucine repeat region, which are identified as the Rho-binding region
The profile we developed covers the entire REM-1 domain.
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