Search results for RND1

Showing 7 results out of 25

×

Species

Types

Compartments

Reaction types

Search properties

Species

Types

Compartments

Reaction types

Search properties

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 seven phylogenetic branches of the Ras superfamily (Bernards 2005), which, besides Rho, Miro and RHOBTB3 also includes Ran, Arf, Rab and Ras families (Boureux et al. 2007). Miro GTPases and RHOBTB3 ATPase are sometimes described as Rho family members, but they are phylogenetically distinct (Boureux et al. 2007). Phylogenetically, RHO GTPases can be grouped into four clusters. The first cluster consists of three subfamilies: Rho, RhoD/RhoF and Rnd. The second cluster consists of three subfamilies: Rac, Cdc42 and RhoU/RhoV. The third cluster consists of the RhoH subfamily. The fourth cluster consists of the RhoBTB subfamily. Based on their activation type, RHO GTPases can be divided into classical (typical) and atypical (reviewed by Haga and Ridley 2016, and Kalpachidou et al. 2019). Classical RHO GTPases cycle between active GTP-bound states and inactive GDP-bound states through steps that are tightly controlled by members of three classes of proteins: (1) guanine nucleotide dissociation inhibitors or GDIs, which maintain Rho proteins in an inactive state in the cytoplasm, (2) guanine nucleotide exchange factors or GEFs, which destabilize the interaction between Rho proteins and their bound nucleotide, the net result of which is the exchange of bound GDP for the more abundant GTP, and (3) GTPase activating proteins or GAPs, which stimulate the low intrinsic GTP hydrolysis activity of Rho family members, thus promoting their inactivation. GDIs, GEFs, and GAPs are themselves subject to tight regulation, and the overall level of Rho activity reflects the balance of their activities. Many of the Rho-specific GEFs, GAPs, and GDIs act on multiple Rho GTPases, so that regulation of these control proteins can have complex effects on the functions of multiple Rho GTPases (reviewed by Van Aelst and D'Souza-Schorey 1997, Schmidt and Hall 2002, Jaffe and Hall 2005, Bernards 2005, and Hodge and Ridley 2016). Classical RHO GTPases include four subfamilies: Rho (includes RHOA, RHOB and RHOC), Rac (includes RAC1, RAC2, RAC3 and RHOG), Cdc42 (includes CDC42, RHOJ and RHOQ) and RhoD/RhoF (includes RHOD and RHOF) (reviewed in Haga and Ridley 2016). Atypical RHO GTPases do not possess GTPase activity. They therefore constitutively exist in the active GTP-bound state. Atypical RHO GTPases include three subfamilies: Rnd (includes RND1, RND2 and RND3), RhoBTB (includes RHOBTB1 and RHOBTB2), RhoH (RHOH is the only member) and RhoU/RhoV (includes RHOU and RHOV). Members of the Rho family have been identified in all eukaryotes. Among Rho GTPases, RHOA, RAC1 and CDC42 have been most extensively studied.

RHO GTPases regulate cell behavior by activating a number of downstream effectors that regulate cytoskeletal organization, intracellular trafficking and transcription (reviewed by Sahai and Marshall 2002). They 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). One of the best studied RHO GTPase effectors are protein kinases ROCK1 and ROCK2, which phosphorylate many proteins involved in the stabilization of actin filaments and generation of actin-myosin contractile force, such as LIM kinases and myosin regulatory light chains (MRLC) (reviewed in Riento and Ridley 2003). The p21-activated kinase family, which includes PAK1, PAK2 and PAK3, is another well characterized family of RHO GTPase effectors involved in cytoskeleton regulation (reviewed in Daniels and Bokoch 1999, Szczepanowska 2009). Protein kinase C related kinases (PKNs), PKN1, PKN2 and PKN3 play important roles in cytoskeleton organization (Hamaguchi et al. 2000), regulation of cell cycle (Misaki et al. 2001), receptor trafficking (Metzger et al. 2003), apoptosis (Takahashi et al. 1998), and transcription (Metzger et al. 2003, Metzger et al. 2005, Metzger et al. 2008). Citron kinase (CIT) is involved in Golgi apparatus organization through regulation of the actin cytoskeleton (Camera et al. 2003) and in the regulation of cytokinesis (Gruneberg et al. 2006, Bassi et al. 2013, Watanabe et al. 2013). Kinectin (KTN1), a kinesin anchor protein, is a RHO GTPase effector involved in kinesin-mediated vesicle motility (Vignal et al. 2001, Hotta et al. 1996), including microtubule-dependent lysosomal transport (Vignal et al. 2001). IQGAP proteins, IQGAP1, IQGAP2 and IQGAP3, are RHO GTPase effectors that modulate cell shape and motility through regulation of G-actin/F-actin equilibrium (Brill et al. 1996, Fukata et al. 1997, Bashour et al. 1997, Wang et al. 2007, Pelikan-Conchaudron et al. 2011), regulate adherens junctions (Kuroda et al. 1998, Hage et al. 2009), and contribute to cell polarity and lamellipodia formation (Fukata et al. 2002, Suzuki and Takahashi 2008). WASP and WAVE proteins (reviewed by Lane et al. 2014), as well as formins (reviewed by Kuhn and Geyer 2014), are RHO GTPase effectors that regulate actin polymerization and play important roles in cell motility, organelle trafficking and mitosis. Rhotekin (RTKN) and rhophilins (RHPN1 and RHPN2) are RHO GTPase effectors that regulate the organization of the actin cytoskeleton and are implicated in the establishment of cell polarity, cell motility and possibly endosome trafficking (Sudo et al. 2006, Watanabe et al. 1996, Fujita et al. 2000, Peck et al. 2002, Mircescu et al. 2002). Cytoskeletal changes triggered by the activation of formins (Miralles et al. 2003) and RTKN (Reynaud et al. 2000) may lead to stimulation of SRF-mediated transcription. NADPH oxidase complexes 1, 2 and 3 (NOX1, NOX2 and NOX3), membrane associated enzymatic complexes that use NADPH as an electron donor to reduce oxygen and produce superoxide (O2-), are also regulated by RHO GTPases (Knaus et al. 1991, Roberts et al. 1999, Kim and Dinauer 2001, Jyoti et al. 2014, Cheng et al. 2006, Miyano et al. 2006, Ueyama et al. 2006). Every RHO GTPase activates multiple downstream effectors and most effectors are regulated by multiple RHO GTPases, resulting in an elaborate cross-talk.

Reaction (5 results from a total of 10)

Identifier: R-HSA-9696268
Species: Homo sapiens
Compartment: cytosol, plasma membrane
Active GTP bound RND3 binds the following effectors:
ARHGAP5 (Wennerberg et al. 2003; Bagci et al. 2020)
KCTD13 (Gladwyn Ng et al. 2016)
PLEKHG5 (Goh and Manser 2010)
ROCK1 (Riento et al. 2003) RND3 inhibits kinase activity of ROCK1
TNFAIP1 (Gladwyn Ng et al. 2016)
UBXN11 (Katoh et al. 2002)

The following candidate RND3 effectors were reported in the high throughput screen by Bagci et al. 2020 or were reported by some but not all studies:
ANKRD26 (Bagci et al. 2020)
ARHGAP21 (Bagci et al. 2020)
ARHGAP35 (Wennerberg et al. 2003: binding to active RND3; Bagci et al. 2020: no binding to active RND3)
CAV1 (Bagci et al. 2020)
CCDC88A (Bagci et al. 2020)
CKAP4 (Bagci et al. 2020)
CKB (Bagci et al. 2020)
CPD (Bagci et al. 2020)
DDX4 (Bagci et al. 2020)
DEPDC1B (Bagci et al. 2020)
DLG5 (Bagci et al. 2020)
DSG1 (Bagci et al. 2020)
DSP (Bagci et al. 2020)
DST (Bagci et al. 2020)
EPHA2 (Bagci et al. 2020)
FAM83B (Bagci et al. 2020)
FLOT2 (Bagci et al. 2020)
KTN1 (Bagci et al. 2020) - RND3 has not been shown to localize to the endoplasmic reticulum membrane, but some isoforms of KTN1 have been shown to localize to the plasma membrane (Santama et al. 2004)
LEMD3 (Bagci et al. 2020)
MUC13 (Bagci et al. 2020)
NISCH (Bagci et al. 2020)
PICALM (Bagci et al. 2020)
PIK3R1 (Bagci et al. 2020)
PIK3R2 (Bagci et al. 2020)
PKP4 (Bagci et al. 2020)
PTPN13 (Bagci et al. 2020)
RASAL2 (Bagci et al. 2020)
RBMX (Bagci et al. 2020)
SCRIB (Bagci et al. 2020)
SEMA4F (Bagci et al. 2020)
TMOD3 (Bagci et al. 2020)
TXNL1 (Bagci et al. 2020)
VANGL1 (Bagci et al. 2020)
VANGL2 (Bagci et al. 2020)
WDR6 (Bagci et al. 2020)

RND3 does not interact with the following effectors:
ALDH3A2 (Bagci et al. 2020)
EPSTI1 (Bagci et al. 2020)
FAM135A (Bagci et al. 2020)
FNBP1 (Bagci et al. 2020)
FRS2 (Harada et al. 2005)
FRS3 (Harada et al. 2003)
GOLGA3 (Bagci et al. 2020)
KIDINS220 (Bagci et al. 2020)
KIF14 (Bagci et al. 2020)
LRRC1 (Bagci et al. 2020)
NUDC (Bagci et al. 2020)
ROCK2 (Riento et al. 2003)
RRAS2 (Bagci et al. 2020)
STMN2 (Li et al. 2009)
TFRC (Bagci et al. 2020)
TMEM59 (Bagci et al. 2020)
UHRF1BP1L (Bagci et al. 2020)
Identifier: R-HSA-9693198
Species: Homo sapiens
Compartment: cytosol, plasma membrane
Active GTP bound RHOD binds to the following effectors at the plasma membrane:
DIAPH1 (Kyrkou et al. 2013)
PAK6 (Durkin et al. 2017)
PLXNA1 (Zanata et al. 2002)
PLXNB1 (Tong et al. 2007)

The following candidate RHOD effectors that can localize to plasma membrane and cytosol were reported in the high throughput screen by Bagci et al. 2020:
ACTN1 (Bagci et al. 2020)
ADD3 (Bagci et al. 2020)
AKAP12 (Bagci et al. 2020)
ARHGAP1 (Bagci et al. 2020)
ARHGAP39 (Bagci et al. 2020)
CAPZB (Bagci et al. 2020)
CAV1 (Bagci et al. 2020)
CPNE8 (Bagci et al. 2020)
DBN1 (Bagci et al. 2020)
DIAPH3 (Bagci et al. 2020)
EFHD2 (Bagci et al. 2020)
ESYT1 (Bagci et al. 2020)
LMNB1 (Bagci et al. 2020)
MCAM (Bagci et al. 2020)
RAB7A (Bagci et al. 2020)
SLC4A7 (Bagci et al. 2020)
STBD1 (Bagci et al. 2020)
STEAP3 (Bagci et al. 2020)
TMPO (Bagci et al. 2020)
TOR1AIP1 (Bagci et al. 2020)
VAMP3 (Bagci et al. 2020)
VANGL1 (Bagci et al. 2020)

The following putative effectors do not bind to active RHOD:
ACTB (Bagci et al. 2020)
BASP1 (Bagci et al. 2020)
FAM169A (Bagci et al. 2020)
MTMR1 (Bagci et al. 2020)
POTEE (Bagci et al. 2020)
SENP1 (Bagci et al. 2020)
SNAP23 (Bagci et al. 2020)
SOWAHC (Bagci et al. 2020)
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-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
Cite Us!