RHOB binds effectors at the plasma membrane

Stable Identifier
R-HSA-9013024
Type
Reaction
Species
Homo sapiens
Compartment
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In its GTP bound active form, plasma membrane associated RHOB (or constitutively active RHOB mutant in the high throughput study by Bagci et al. 2020) binds to the following effectors at the plasma membrane:
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)
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)

The following putative RHOB effectors were identified only in the high throughput study by Bagci et al. 2020, where they were shown to bind to the active mutant of RHOB, and are annotated as candidate RHOB effectors:
ACTC1 (Bagci et al. 2020)
ANLN (Bagci et al. 2020)
ARHGAP1 (Bagci et al. 2020)
BCR (Bagci et al. 2020)
CAV1 (Bagci et al. 2020)
CAVIN1 (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)
IQGAP3 (Bagci et al. 2020)
JUP (Bagci et al. 2020)
MCAM (Bagci et al. 2020)
MYO9B (Bagci et al. 2020)
PCDH7 (Bagci et al. 2020)
SLK (Bagci et al. 2020)
SNAP23 (Bagci et al. 2020)
SOWAHC (Bagci et al. 2020)
STK10 (Bagci et al. 2020)
STOM (Bagci et al. 2020)
TFRC (Bagci et al. 2020)
TJP2 (Bagci et al. 2020)
VAMP3 (Bagci et al. 2020)
VANGL1 (Bagci et al. 2020)

Active RHOB does not bind the following effectors:
AAAS (Bagci et al. 2020)
ABCD3 (Bagci et al. 2020)
ACBD5 (Bagci et al. 2020)
ATP6AP1 (Bagci et al. 2020)
BCAP31 (Bagci et al. 2020)
C1QBP (Bagci et al. 2020)
CCDC115 (Bagci et al. 2020)
CCDC187 (Bagci et al. 2020)
DDRGK1 (Bagci et al. 2020)
EMC3 (Bagci et al. 2020)
FAF2 (Bagci et al. 2020)
FMNL2 (Kitzing et al. 2010)
FMNL3 (Bagci et al. 2020)
HMOX2 (Bagci et al. 2020)
IQGAP1 (Casteel et al. 2012)
KIAA0355 (Bagci et al. 2020)
LBR (Bagci et al. 2020)
MACO1 (Bagci et al. 2020)
LMAN1 (Bagci et al. 2020)
PGRMC2 (Bagci et al. 2020)
RHOA (Bagci et al. 2020)
SCFD1 (Bagci et al. 2020)
STBD1 (Bagci et al. 2020)
STX5 (Bagci et al. 2020)
TEX2 (Bagci et al. 2020)
TMEM87A (Bagci et al. 2020)
TMPO (Bagci et al. 2020)
VAPB (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

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

Biochemistry 2013
9792683 Citron rho-interacting kinase, a novel tissue-specific ser/thr kinase encompassing the Rho-Rac-binding protein Citron

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

J. Biol. Chem. 1998
20101212 Formin-like 2 drives amoeboid invasive cell motility downstream of RhoC

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

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

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

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

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

J. Biol. Chem. 1996
22992742 Rho isoform-specific interaction with IQGAP1 promotes breast cancer cell proliferation and migration

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

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

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

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

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

J. Biol. Chem. 2008
8543060 A novel partner for the GTP-bound forms of rho and rac

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

FEBS Lett. 1995
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