RND1 binds effectors

Stable Identifier
R-HSA-9696271
Type
Reaction [binding]
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
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Active GTP-bound RND1 binds the following effectors:
ARHGAP5 (Wennerberg et al. 2003; Bagci et al. 2020)
FRS2 (Harada et al. 2005)
FRS3 (Harada et al. 2005)
GRB7 (Vayssiere et al. 2000)
PLEKHG5 (Goh and Manser 2010)
PLXNA1 (Zanata et al. 2002)
STIP1 (de Souza et al. 2014)
STMN2 (Li et al. 2009)
UBXN11 (Katoh et al. 2002)

The following candidate RND1 effectors were reported in the high throughput screen by Bagci et al. 2020 or have been reported as RND1 effectors in some but not all studies:
ALDH3A2 (Bagci et al. 2020)
ANKRD26 (Bagci et al. 2020)
ARHGAP35 (Wennerberg et al. 2003, Mori et al. 2009: binding to active RND1; Bagci et al. 2020: no binding to active RND1)
CAV1 (Bagci et al. 2020)
CCDC88A (Bagci et al. 2020)
CPD (Bagci et al. 2020)
DEPDC1B (Bagci et al. 2020)
DLG5 (Bagci et al. 2020)
DSP (Bagci et al. 2020)
DST (Bagci et al. 2020)
EPHA2 (Bagci et al. 2020)
EPSTI1 (Bagci et al. 2020)
FAM135A (Bagci et al. 2020)
FAM83B (Bagci et al. 2020)
FLOT2 (Bagci et al. 2020)
KIDINS220 (Bagci et al. 2020)
KIF14 (Bagci et al. 2020)
LEMD3 (Bagci et al. 2020)
MUC13 (Bagci et al. 2020)
PKP4 (Bagci et al. 2020)
PIK3R1 (Bagci et al. 2020)
PIK3R2 (Bagci et al. 2020)
PTPN13 (Bagci et al. 2020)
RASAL2 (Bagci et al. 2020)
RBMX (Bagci et al. 2020)
RRAS2 (Bagci et al. 2020)
TFRC (Bagci et al. 2020)
TMEM59 (Bagci et al. 2020)
TXNL1 (Bagci et al. 2020)
VANGL1 (Bagci et al. 2020)
VANGL2 (Bagci et al. 2020)
WDR6 (Bagci et al. 2020)

RND1 does not interact with the following putative effectors that bind to active RND2 and/or RND3:
CKAP4 (Bagci et al. 2020)
CKB (Bagci et al. 2020)
DDX4 (Bagci et al. 2020)
DSG1 (Bagci et al. 2020)
FNBP1 (Bagci et al. 2020)
GOLGA3 (Bagci et al. 2020)
KTN1 (Bagci et al. 2020)
LRRC1 (Bagci et al. 2020)
NISCH (Bagci et al. 2020)
NUDC (Bagci et al. 2020)
PICALM (Bagci et al. 2020)
SCRIB (Bagci et al. 2020)
SEMA4F (Bagci et al. 2020)
TMOD3 (Bagci et al. 2020)
UHRF1BP1L (Bagci et al. 2020)

Literature References
PubMed ID Title Journal Year
15738000 Direct interaction of Rnd1 with FRS2 beta regulates Rnd1-induced down-regulation of RhoA activity and is involved in fibroblast growth factor-induced neurite outgrowth in PC12 cells

Harada, A, Katoh, H, Negishi, M

J. Biol. Chem. 2005
24690281 STI1 antagonizes cytoskeleton collapse mediated by small GTPase Rnd1 and regulates neurite growth

de Souza, LE, Moura Costa, MD, Bilek, ES, Lopes, MH, Martins, VR, Püschel, AW, Mercadante, AF, Nakao, LS, Zanata, SM

Exp. Cell Res. 2014
11784792 Antagonistic effects of Rnd1 and RhoD GTPases regulate receptor activity in Semaphorin 3A-induced cytoskeletal collapse

Zanata, SM, Hovatta, I, Rohm, B, Püschel, AW

J Neurosci 2002
11940653 Socius is a novel Rnd GTPase-interacting protein involved in disassembly of actin stress fibers

Katoh, H, Harada, A, Mori, K, Negishi, M

Mol. Cell. Biol. 2002
20811643 The RhoA GEF Syx is a target of Rnd3 and regulated via a Raf1-like ubiquitin-related domain

Goh, LL, Manser, E

PLoS ONE 2010
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
10664463 Interaction of the Grb7 adapter protein with Rnd1, a new member of the Rho family

Vayssière, B, Zalcman, G, Mahé, Y, Mirey, G, Ligensa, T, Weidner, KM, Chardin, P, Camonis, J

FEBS Lett. 2000
18996843 Rnd1 regulates axon extension by enhancing the microtubule destabilizing activity of SCG10

Li, YH, Ghavampur, S, Bondallaz, P, Will, L, Grenningloh, G, Püschel, AW

J. Biol. Chem. 2009
12842009 Rnd proteins function as RhoA antagonists by activating p190 RhoGAP

Wennerberg, K, Forget, MA, Ellerbroek, SM, Arthur, WT, Burridge, K, Settleman, J, Der, CJ, Hansen, SH

Curr. Biol. 2003
19103606 Rho-kinase contributes to sustained RhoA activation through phosphorylation of p190A RhoGAP

Mori, K, Amano, M, Takefuji, M, Kato, K, Morita, Y, Nishioka, T, Matsuura, Y, Murohara, T, Kaibuchi, K

J. Biol. Chem. 2009
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