ARHGAP32
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Official Full Name
Rho GTPase activating protein 32
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Overview
RICS is a neuron-associated GTPase-activating protein that may regulate dendritic spine morphology and strength by;modulating Rho GTPase (see RHOA; MIM 165390) activity (Okabe et al., 2003 (PubMed 12531901)). -
Synonyms
ARHGAP32; Rho GTPase activating protein 32; rho GTPase-activating protein 32; GC GAP; GRIT; KIAA0712; MGC1892; RICS; GAB-associated CDC42; rac GTPase activating protein; rho-type GTPase-activating protein 32; GTPase regulator interacting with TrkA; brain-;
Species | Cat.# | Product name | Source (Host) | Tag | Protein Length | Price |
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Mouse | ARHGAP32-1871M | Recombinant Mouse ARHGAP32 Protein | Mammalian Cell | His | ||
Mouse | ARHGAP32-680M-B | Recombinant Mouse ARHGAP32 Protein Pre-coupled Magnetic Beads | HEK293 | |||
Mouse | ARHGAP32-680M | Recombinant Mouse ARHGAP32 Protein, His (Fc)-Avi-tagged | HEK293 | His (Fc)-Avi |
- Involved Pathway
- Protein Function
- Interacting Protein
ARHGAP32 involved in several pathways and played different roles in them. We selected most pathways ARHGAP32 participated on our site, such as Rho GTPase cycle, Signal Transduction, Signaling by Rho GTPases, which may be useful for your reference. Also, other proteins which involved in the same pathway with ARHGAP32 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name | Pathway Related Protein |
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Rho GTPase cycle | STARD13;ARHGAP36;RALBP1;FAM13B1;ARAP2;TAGAPB;ARHGAP8;FGD2;ARHGAP20 |
Signal Transduction | NOG1;RNF43;SEPT7;TAC3;GPR120;ABHD6B;SHARPIN;DHRS9;ARHGAP25 |
Signaling by Rho GTPases | ARHGAP11A;RTKN;ARHGAP17;ARHGAP23;ARHGEF16;ARHGAP9;ARHGAP10;ARHGAP33;TAGAP1 |
XPodNet - protein-protein interactions in the podocyte expanded by STRING | TSSK5;Ighg;OASL2;SNTB1;WLS;ZFP423;FLII;CMIP;KCP |
ARHGAP32 has several biochemical functions, for example, GTPase activator activity, phosphatidylinositol binding. Some of the functions are cooperated with other proteins, some of the functions could acted by ARHGAP32 itself. We selected most functions ARHGAP32 had, and list some proteins which have the same functions with ARHGAP32. You can find most of the proteins on our site.
Function | Related Protein |
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GTPase activator activity | RANGAP1B;TBC1D30;RAP1GAP;FAM13A;TBC1D3C;ALDH1A2;RINL;RGS9;RGS13 |
phosphatidylinositol binding | SNX33;SNX29;NISCH;SNX2;FCHO2;SNX9B;P2RX2;MTM1;SGK3 |
ARHGAP32 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with ARHGAP32 here. Most of them are supplied by our site. Hope this information will be useful for your research of ARHGAP32.
GABRB2
- Q&As
- Reviews
Q&As (31)
Ask a questionYes, ARHGAP32 may have additional roles in different cellular processes that are yet to be fully explored. Its interactions with various proteins and its wide expression pattern suggest that it may participate in diverse cellular functions beyond the currently known roles.
Currently, there are no specific small molecules or drugs known to directly interact with ARHGAP32. However, targeting ARHGAP32-related signaling pathways or downstream effector proteins may indirectly affect its activity and function.
Current research suggests that ARHGAP32 may play a role in cancer progression and metastasis. It has been found to be dysregulated in certain cancer types, and its overexpression or silencing has been associated with altered cellular processes related to cancer, including migration, invasion, and angiogenesis. Further studies are needed to fully understand the extent of ARHGAP32's involvement in cancer.
Yes, ARHGAP32 plays a crucial role in neuronal development and function. It is highly expressed in the brain and is involved in processes such as axon guidance, neurite outgrowth, and dendritic spine formation. ARHGAP32 also contributes to synaptic plasticity and neurotransmitter release.
Mutations or alterations in ARHGAP32 have been implicated in various human diseases and conditions. For example, changes in ARHGAP32 expression have been observed in schizophrenia patients. Some studies have also linked ARHGAP32 polymorphisms to an increased risk of developing neurodevelopmental disorders such as autism spectrum disorders.
ARHGAP32 regulates Rho GTPase signaling by acting as a RhoGAP protein. It binds to the active, GTP-bound form of Rho GTPases and stimulates their intrinsic GTPase activity. This catalyzes the hydrolysis of GTP to GDP, leading to the inactivation of Rho GTPases. By promoting the transition of Rho GTPases from the active to the inactive state, ARHGAP32 negatively regulates their signaling and downstream effector pathways.
ARHGAP32 is expressed in a wide range of cell types and tissues. Its expression can vary depending on the cell type and developmental stage. While ARHGAP32 is most prominently expressed in the nervous system, it is also found in immune cells, fibroblasts, epithelial cells, and many other cell types. Its expression pattern suggests diverse cellular functions in different tissues and contexts.
Yes, several studies have suggested a role for ARHGAP32 in cancer progression. It has been found to be upregulated or downregulated in various types of cancer, and its dysregulation has been associated with tumor cell migration, invasion, and metastasis. ARHGAP32's involvement in regulating Rho GTPase activity and cytoskeletal dynamics may contribute to cancer cell motility and the acquisition of invasive phenotypes.
ARHGAP32 can interact with several proteins involved in cytoskeletal remodeling, cell adhesion, and signaling pathways. Some known binding partners include p190RhoGAP, paxillin, focal adhesion kinase (FAK), and NMDA receptors.
ARHGAP32 can localize to multiple subcellular compartments, including the plasma membrane, cytoplasm, and the nucleus. Its subcellular localization may vary depending on cell type and signaling context.
Studies in animal models have suggested that ARHGAP32 plays a role in embryonic development. Mice lacking the ARHGAP32 gene show defects in neuronal development, including impaired axon guidance and hippocampal formation, suggesting an essential role for ARHGAP32 during embryogenesis.
Currently, there are no specific drugs or compounds available that directly target ARHGAP32. However, some compounds that influence Rho GTPase signaling pathways may indirectly affect ARHGAP32 activity. For example, small molecules targeting Rho GTPases or their upstream regulators can modulate the activity of ARHGAP32.
ARHGAP32 interacts with proteins such as paxillin and focal adhesion kinase (FAK), which are part of cell adhesion complexes. These interactions can regulate the turnover and dynamics of focal adhesions, which are crucial for cell adhesion, migration, and the transmission of mechanical forces. ARHGAP32's activity influences the balance between focal adhesion assembly and disassembly by modulating Rho GTPase signaling pathways within the adhesion complex.
ARHGAP32 primarily functions as a regulator of Rho GTPase activity and downstream signaling pathways. While it may indirectly influence gene expression through its effects on cytoskeletal dynamics and cellular processes, its direct involvement in gene regulation is less understood compared to its role in Rho GTPase regulation. Further research is needed to explore the potential gene regulatory functions of ARHGAP32.
Yes, animal models, particularly mice, with genetic modifications of the ARHGAP32 gene have been generated. These models have provided valuable insights into the role of ARHGAP32 in neuronal development and function.
ARHGAP32 has been implicated in various diseases and pathological conditions. Dysregulation of ARHGAP32 has been associated with cancer progression, neurodevelopmental disorders, neurodegenerative diseases, and cardiovascular disorders, among others.
Yes, alternative splicing of the ARHGAP32 gene can lead to the generation of different isoforms. These isoforms may exhibit distinct functional properties or tissue-specific expression patterns.
Yes, ARHGAP32 contains several conserved structural domains, including a RhoGAP domain, SH3 domains, and an F-actin binding domain. These domains contribute to its ability to regulate Rho GTPase signaling and interact with other proteins.
Yes, ARHGAP32 interacts with several proteins and signaling pathways. It can associate with other Rho GTPase regulators, scaffold proteins, and cytoskeletal components. ARHGAP32 is also regulated by various signaling cascades, including tyrosine kinases, calcium signaling, and neurotransmitter receptors.
ARHGAP32 acts as a RhoGAP, which means it enhances the intrinsic GTPase activity of Rho family GTPases such as RhoA, Rac1, and Cdc42. By doing so, it negatively regulates their signaling by promoting their transition from the active, GTP-bound state to the inactive, GDP-bound state.
ARHGAP32 is highly expressed in neurons and plays important roles in neuronal development and synaptic function. It regulates axon guidance, dendritic arborization, spine morphology, and synaptic plasticity through its interactions with cytoskeletal and signaling proteins.
Mutations or altered expression of ARHGAP32 have been implicated in neurodevelopmental disorders such as autism spectrum disorders (ASD) and intellectual disability. These disorders are characterized by impairments in social interaction, communication, and cognitive function. ARHGAP32's role in neuronal development, axon guidance, and synaptic plasticity suggests its potential involvement in the pathogenesis of these disorders.
The downstream effectors of Rho GTPases regulated by ARHGAP32 are diverse and depend on the specific Rho GTPase involved. For example, RhoA signaling can activate ROCK (Rho-associated coiled-coil-containing protein kinase), which regulates actomyosin contractility and stress fiber formation. Rac1 activation can lead to the activation of WAVE (Wiskott-Aldrich syndrome protein family verprolin-homologous protein), promoting actin polymerization and lamellipodia formation. Cdc42 activation can activate N-WASP (Neuronal Wiskott-Aldrich syndrome protein), leading to actin polymerization and filopodia formation.
By regulating Rho GTPases, ARHGAP32 influences actin cytoskeleton organization and dynamics. It promotes the disassembly of actin stress fibers and focal adhesions by inhibiting RhoA activity, leading to cytoskeletal rearrangements and changes in cell morphology.
Due to its involvement in various diseases, ARHGAP32 has been considered as a potential therapeutic target. Modulating the activity of ARHGAP32 or its downstream pathways may offer therapeutic benefits in certain conditions, such as neurodevelopmental disorders or neurological injuries.
Yes, ARHGAP32 can undergo post-translational modifications, including phosphorylation and palmitoylation. These modifications can regulate its activity and subcellular localization.
ARHGAP32 has emerged as a potential therapeutic target in certain diseases, including cancer and neurodevelopmental disorders. Modulating its activity or expression may hold therapeutic potential, but further research is needed to determine the feasibility and efficacy of such interventions.
Yes, genetic variations and mutations in ARHGAP32 have been associated with various diseases. For example, specific mutations in ARHGAP32 have been linked to developmental anomalies like gray platelet syndrome and Temtamy syndrome, which are characterized by abnormalities in platelet production and development. Further research is needed to understand the full extent of genetic variations in ARHGAP32 and their implications for disease.
ARHGAP32 can be detected or measured using techniques such as Western blotting, immunofluorescence microscopy, or immunoprecipitation followed by mass spectrometry. Antibodies specific to ARHGAP32 are commonly used to probe its expression and localization.
ARHGAP32 is expressed in various cell types, including neurons, fibroblasts, endothelial cells, and immune cells.
ARHGAP32 is evolutionarily conserved across different species, indicating its functional importance. The RhoGAP domain and other structural motifs within ARHGAP32 are highly conserved, suggesting their critical roles in cellular processes.
Customer Reviews (8)
Write a reviewThe ARHGAP32 protein surpasses expectations in terms of quality and is an ideal match for my experimental requirements.
By using ARHGAP32 protein, I can explore the mechanisms underlying cell division, cell cycle control, and the molecular pathways associated with these processes.
Its reliability, versatility, and ability to deliver clear and reliable results make it a top choice for researchers in need of a high-quality protein for their experiments.
One major advantage of ARHGAP32 protein is its ability to contribute to the understanding of diseases related to aberrant cell cycle regulation, including cancer.
This enhanced visibility and distinctness of the protein bands greatly aided in the accurate analysis and interpretation of my Western Blotting results.
Its impeccable purity and integrity make it a valuable asset in my research endeavors.
As a researcher utilizing ARHGAP32 protein in my trials, I can highlight its advantages and the valuable support provided by the manufacturer in facilitating my research.
The protein's interaction with other APC/C subunits enables the study of its function and the investigation of its involvement in various cellular processes.
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