RHOC binds effectors at the plasma membrane

Stable Identifier
Reaction [binding]
Homo sapiens
Locations in the PathwayBrowser
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

In its GTP bound active form, plasma membrane associated RHOC binds to the following cytosolic and plasma membrane effectors:
CIT (Madaule et al. 1995; Bagci et al. 2020) and its neuron specific isoform CIT 3 (Di Cunto et al. 1998)
DAAM1 (Higashi et al. 2008)
DIAPH1 (Higashi et al. 2008)
FMNL2 (Kitzing et al. 2010, Moriya et al. 2012)
IQGAP1 (Casteel et al. 2012)
PKN1 (Hutchinson et al. 2013)
PKN2 (Hutchinson et al. 2013, Bagci et al. 2020)
PKN3 (Hutchinson et al. 2013)
ROCK1 (Leung et al. 1996, Bagci et al. 2020)
ROCK2 (Leung et al. 1996, Bagci et al. 2020)
RTKN (Reid et al. 1996)

Opposing findings have been reported on the following putative RHOC effectors, or they were identified only in the high throughput study by Bagci et al. 2020, where they were shown to bind to the active mutant of RHOC; they are therefore annotated as candidate RHOC effectors:
ABCD3 (Bagci et al. 2020)
ACBD5 (Bagci et al. 2020)
ANLN (Bagci et al. 2020)
ARHGAP1 (Bagci et al. 2020)
BCR (Bagci et al. 2020)
C1QBP (Bagci et al. 2020)
CAV1 (Bagci et al. 2020)
CAVIN1 (Bagci et al. 2020)
CCDC187 (Bagci et al. 2020)
DEPDC1B (Bagci et al. 2020)
DIAPH3 (Bagci et al. 2020)
ERBIN (Bagci et al. 2020)
FLOT1 (Bagci et al. 2020)
FLOT2 (Bagci et al. 2020)
FMNL3 (Vega et al. 2011: binds to activated RHOC; Bagci et al. 2020: does not bind to active RHOC)
IQGAP3 (Bagci et al. 2020)
JUP (Bagci et al. 2020)
MCAM (Bagci et al. 2020)
MYO9B (Bagci et al. 2020)
RHOA (Bagci et al. 2020)
SLK (Bagci et al. 2020)
STBD1 (Bagci et al. 2020)
STK10 (Bagci et al. 2020)
STOM (Bagci et al. 2020)
TJP2 (Bagci et al. 2020)
TFRC (Bagci et al. 2020)
TMPO (Bagci et al. 2020)
VAMP3 (Bagci et al. 2020)
VANGL1 (Bagci et al. 2020)

Active RHOC does not bind to
AAAS (Bagci et al. 2020)
ACTC1 (Bagci et al. 2020)
ATP6AP1 (Bagci et al. 2020)
BCAP31 (Bagci et al. 2020)
CCDC115 (Bagci et al. 2020)
DDRGK1 (Bagci et al. 2020)
EMC3 (Bagci et al. 2020)
FAF2 (Bagci et al. 2020)
HMOX2 (Bagci et al. 2020)
KIAA0355 (Bagci et al. 2020)
PCDH7 (Bagci et al. 2020)
SCFD1 (Bagci et al. 2020)
SNAP23 (Bagci et al. 2020)
SOWAHC (Bagci et al. 2020)
TEX2 (Bagci et al. 2020)
TMEM87A (Bagci et al. 2020)
FMNL3 (Bagci et al. 2020)
YKT6 (Bagci et al. 2020)

Literature References
PubMed ID Title Journal Year
9792683 Citron rho-interacting kinase, a novel tissue-specific ser/thr kinase encompassing the Rho-Rac-binding protein Citron

Di Cunto, F, Calautti, E, Hsiao, J, Ong, L, Topley, G, Turco, E, Dotto, GP

J. Biol. Chem. 1998
24128008 Differential binding of RhoA, RhoB, and RhoC to protein kinase C-related kinase (PRK) isoforms PRK1, PRK2, and PRK3: PRKs have the highest affinity for RhoB

Hutchinson, CL, Lowe, PN, McLaughlin, SH, Mott, HR, Owen, D

Biochemistry 2013
20101212 Formin-like 2 drives amoeboid invasive cell motility downstream of RhoC

Kitzing, TM, Wang, Y, Pertz, O, Copeland, JW, Grosse, R

Oncogene 2010
8816443 The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton

Leung, T, Chen, XQ, Manser, E, Lim, L

Mol. Cell. Biol. 1996
8662891 Rhotekin, a new putative target for Rho bearing homology to a serine/threonine kinase, PKN, and rhophilin in the rho-binding domain

Reid, T, Furuyashiki, T, Ishizaki, T, Watanabe, G, Watanabe, N, Fujisawa, K, Morii, N, Madaule, P, Narumiya, S

J. Biol. Chem. 1996
21576392 RhoA and RhoC have distinct roles in migration and invasion by acting through different targets

Vega, FM, Fruhwirth, G, Ng, T, Ridley, AJ

J. Cell Biol. 2011
22992742 Rho isoform-specific interaction with IQGAP1 promotes breast cancer cell proliferation and migration

Casteel, DE, Turner, S, Schwappacher, R, Rangaswami, H, Su-Yuo, J, Zhuang, S, Boss, GR, Pilz, RB

J. Biol. Chem. 2012
31871319 Mapping the proximity interaction network of the Rho-family GTPases reveals signalling pathways and regulatory mechanisms

Bagci, H, Sriskandarajah, N, Robert, A, Boulais, J, Elkholi, IE, Tran, V, Lin, ZY, Thibault, MP, Dubé, N, Faubert, D, Hipfner, DR, Gingras, AC, Cote, JF

Nat. Cell Biol. 2020
18218625 Biochemical characterization of the Rho GTPase-regulated actin assembly by diaphanous-related formins, mDia1 and Daam1, in platelets

Higashi, T, Ikeda, T, Shirakawa, R, Kondo, H, Kawato, M, Horiguchi, M, Okuda, T, Okawa, K, Fukai, S, Nureki, O, Kita, T, Horiuchi, H

J. Biol. Chem. 2008
22790947 Protein N-myristoylation is required for cellular morphological changes induced by two formin family proteins, FMNL2 and FMNL3

Moriya, K, Yamamoto, T, Takamitsu, E, Matsunaga, Y, Kimoto, M, Fukushige, D, Kimoto, C, Suzuki, T, Utsumi, T

Biosci. Biotechnol. Biochem. 2012
8543060 A novel partner for the GTP-bound forms of rho and rac

Madaule, P, Furuyashiki, T, Reid, T, Ishizaki, T, Watanabe, G, Morii, N, Narumiya, S

FEBS Lett. 1995
Orthologous Events
Cite Us!