Search results for RND1

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Pathway (1 results from a total of 6)

Identifier: R-HSA-194315
Species: Homo sapiens
The Rho family of small guanine nucleotide binding proteins is one of five generally recognized branches of the Ras superfamily. Like most Ras superfamily members, typical Rho proteins function as binary switches controlling a variety of biological processes. They perform this function by cycling between active GTP-bound and inactive GDP-bound conformations. Mammalian Rho GTPases include RhoA, RhoB and RhoC (Rho proteins), Rac1 3 (Rac proteins), Cdc42, TC10, TCL, Wrch1, Chp/Wrch2, RhoD and RhoG, to name some. The family also includes RhoH and Rnd1-3, which lack GTPase activity and are predicted to exist in a constitutively active state.

Members of the Rho family have been identified in all eukaryotes. Including the atypical RHOBTB1-3 and RHOT1-2 proteins, 24 Rho family members have been identified in mammals (Jaffe and Hall, 2005; Bernards, 2005; Ridley, 2006). Among Rho GTPases, RhoA, Rac1 and Cdc42 have been most extensively studied. These proteins are best known for their ability to induce dynamic rearrangements of the plasma membrane-associated actin cytoskeleton (Aspenstrom et al, 2004; Murphy et al, 1999; Govek et al, 2005). Beyond this function, Rho GTPases also regulate actomyosin contractility and microtubule dynamics. Rho mediated effects on transcription and membrane trafficking are believed to be secondary to these functions. At the more macroscopic level, Rho GTPases have been implicated in many important cell biological processes, including cell growth control, cytokinesis, cell motility, cell cell and cell extracellular matrix adhesion, cell transformation and invasion, and development (Govek et al., 2005). The illustration below lists Rho GTPase effectors implicated in actin and microtubule dynamics (courtesy: Govek et al., 2005, Genes and Development, CSHL Press).

Reaction (4 results from a total of 9)

Identifier: R-HSA-416588
Species: Homo sapiens
Compartment: cytosol, plasma membrane
The RhoGEFs LARG and PDZ-RhoGEF complexed with Plexin-B1 stimulate the exchange of GDP for GTP on RhoA through their DH and PH domains.
Identifier: R-HSA-9696266
Species: Homo sapiens
Compartment: cytosol, plasma membrane
Active GTP bound RND2 binds the following effectors:
ARHGAP5 (Wennerberg et al. 2003; Bagi et al. 2020)
FNBP1 (Fujita et al. 2002; Kakimoto et al. 2004; Bagci et al. 2020)
FRS2 (Harada et al. 2005)
FRS3 (Harada et al. 2005)
KCTD13 (Gladwyn Ng et al. 2016)
PLXND1 (Uesugi et al. 2009)
PRAG1 (Tanaka et al. 2006)
TNFAIP1 (Gladwyn Ng et al. 2015; Gladwyn Ng et al. 2016)
UBXN11 (Katoh et al. 2002)

RND2 binds to the following candidate effectors reported in the high throughput screen by Bagci et al. 2020 or reported in some but all studies:
ALDH3A2 (Bagci et al. 2020)
ANKRD26 (Bagci et al. 2020)
ARHGAP1 (Bagci et al. 2020)
ARHGAP35 (Wennerberg et al. 2003: binding to active RND2; Bagci et al. 2020: no binding to active RND2)
CAV1 (Bagci et al. 2020)
CKAP4 (Bagci et al. 2020)
DEPDC1B (Bagci et al. 2020)
DLG5 (Bagci et al. 2020)
DSG1 (Bagci et al. 2020)
DST (Bagci et al. 2020)
EPHA2 (Bagci et al. 2020)
FAM83B (Bagci et al. 2020)
GOLGA3 (Bagci et al. 2020)
KIDINS220 (Bagci et al. 2020)
KIF14 (Bagci et al. 2020)
KTN1 (Bagci et al. 2020) - while RND2 has not been shown to localize to the endoplasmic reticulum membrane (ER), some isoforms of KTN1 are known to localize to the plasma membrane instead of the ER membrane (Santama et al. 2004)
LEMD3 (Bagci et al. 2020)
LRRC1 (Bagci et al. 2020)
MUC13 (Bagci et al. 2020)
NISCH (Bagci et al. 2020)
NUDC (Bagci et al. 2020)
PIK3R1 (Bagci et al. 2020)
PIK3R2 (Bagci et al. 2020)
PKP4 (Bagci et al. 2020)
PTPN13 (Bagci et al. 2020)
RBMX (Bagci et al. 2020)
SCRIB (Bagci et al. 2020)
TFRC (Bagci et al. 2020)
TXNL1 (Bagci et al. 2020)
UHRF1BP1L (Bagci et al. 2020)
VANGL1 (Bagci et al. 2020)
VANGL2 (Bagci et al. 2020)
WDR6 (Bagci et al. 2020)

RND2 does not bind the following effectors:
CCDC88A (Bagci et al. 2020)
CKB (Bagci et al. 2020)
CPD (Bagci et al. 2020)
DDX4 (Bagci et al. 2020)
DSP (Bagci et al. 2020)
EPSTI1 (Bagci et al. 2020)
FAM135A (Bagci et al. 2020)
FLOT2 (Bagci et al. 2020)
GRB7 (Vayssiere et al. 2000)
PLEKHG5 (Goh and Manser 2010)
PICALM (Bagci et al. 2020)
RASAL2 (Bagci et al. 2020)
RRAS2 (Bagci et al. 2020)
SEMA4F (Bagci et al. 2020)
STIP1 (de Souza et al. 2014)
STMN2 (Li et al. 2009)
TMEM59 (Bagci et al. 2020)
TMOD3 (Bagci et al. 2020)
Identifier: R-HSA-416594
Species: Homo sapiens
Compartment: cytosol, plasma membrane
Plexin-B1 activates RhoA and induces growth cone collapse and and cytoskeletal reorganization through Rho-specific guanine nucleotide exchange factors PDZ-RhoGEF (ARHGEF11) and leukemia-associated RhoGEF (LARG, ARHGEF12). Plexin-B1 directly interacts with PDZ-RhoGEF through its c-terminal PDZ domain binding motif. It has been suggested that Rnd1, which binds to the cytoplasmic part of plexin-B1, can promote the interaction between plexin-B1 and PDZ-RhoGEF. The PDZ domain of LARG is directly involved in the interaction with the c-terminal sequence of Plexin-B1.
Identifier: R-HSA-399938
Species: Homo sapiens
Compartment: cytosol
Sema3A-mediated dissociation of FARP2 from Plexin-A is followed by activation of Rac1 by the GEF activity of released FARP2.
FARP2 is critical for Sema3A-mediated axonal repulsion through two independent downstream signaling pathways. Sema3A mediated disassociation of FARP2 from Plexin-A is followed by activation of Rac by GEF activity of released FARP2, binding of Rnd1 to plexin-A and down regulation of R-Ras by GAP activity of plexin-A.

Complex (1 results from a total of 6)

Identifier: R-HSA-416580
Species: Homo sapiens
Compartment: plasma membrane
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