Reactome | RHOC binds effectors at the plasma membrane

RHOC binds effectors at the plasma membrane

Stable Identifier

R-HSA-9013110

Type

Reaction [binding]

Species

Homo sapiens

Compartment

plasma membrane, cytosol

ReviewStatus

5/5

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RHOC binds effectors at the plasma membrane

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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
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
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
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