Regulation of P53 and Cellular Processes By RhoA (G387)

Target Name: RHOA

NCBI ID: G387

RHOA

Regulation of P53 and Cellular Processes By RhoA

Ras (Ras-related Homolog A) is a gene that encodes a protein involved in cell signaling pathways, specifically the RAS/MAPK pathway. This pathway regulates various cellular processes, including cell growth, differentiation, and survival. The RAS/MAPK pathway is a well-established target for many drugs, including anti-cancer agents, and it is expected to be a promising drug target for future therapeutic interventions.

The RAS/MAPK pathway is a complex signaling pathway that involves the recruitment of several transcription factors, including RAF (relative and activated gene 1), MAPK1 (MAPK1), MAPK2 (MAPK2), and MAPK3 (MAPK3). These transcription factors recruit the protein kinase Ak (MAPK), which then phosphorylates various target genes, leading to the downstream regulation of various cellular processes.

One of the protein products of the RAS/MAPK pathway is RhoA, also known as RhoA2, RhoA3, or RhoA4. RhoA is a small GTPase (GTPase is a type of protein that uses GTP (adenylyl cyclic monophosphate) as a ligand) that is involved in the regulation of cell signaling pathways, including the RAS/MAPK pathway.

The RhoA protein is composed of several domains, including an N-terminal transmembrane domain, a catalytic domain, and a C-terminal T-loop domain. The N-terminal transmembrane domain is responsible for the protein's ability to interact with various signaling molecules, including the RAS and MAPK proteins. The catalytic domain is responsible for the protein's catalytic activity, specifically its ability to activate the MAPK pathway. The C-terminal T-loop domain is responsible for the protein's ability to interact with various signaling molecules, including the RAS and MAPK proteins.

RhoA is a protein that plays a crucial role in the regulation of cellular processes, including cell growth, differentiation, and survival. It is a key player in the RAS/MAPK pathway, and its levels are regulated by various signaling pathways. One of the signaling pathways that RhoA is involved in is the cell survival signaling pathway.

In the cell survival signaling pathway, RhoA is involved in the regulation of the survival protein p53. The p53 protein is a well-established tumor suppressor protein that is involved in the regulation of various cellular processes, including cell growth, apoptosis (programmed cell death ), and DNA repair. The p53 protein is composed of several domains, including an N-terminal transmembrane domain, a catalytic domain, and a C-terminal T-loop domain.

The p53 protein is composed of several domains, including an N-terminal transmembrane domain, a catalytic domain, and a C-terminal T-loop domain. The N-terminal transmembrane domain is responsible for the protein's ability to interact with various signaling molecules, including the RAS and MAPK proteins. The catalytic domain is responsible for the protein's catalytic activity, specifically its ability to activate the MAPK pathway. The C-terminal T-loop domain is responsible for the protein's ability to interact with various signaling molecules, including the RAS and MAPK proteins.

RhoA is a protein that is involved in the regulation of the p53 protein. It does this by interacting with the p53 protein and regulating its activity. This interaction between RhoA and p53 is critical for the regulation of cellular processes, including cell growth, apoptosis, and DNA repair.

Another signaling pathway that is regulated by RhoA is the cell cycle signaling pathway. The cell cycle is the process by which cells grow, divide, and replicate their genetic material. The cell cycle signaling pathway is responsible for regulating the cell cycle, and it is composed of several signaling pathways

Protein Name: Ras Homolog Family Member A

Functions: Small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. Mainly associated with cytoskeleton organization, in active state binds to a variety of effector proteins to regulate cellular responses such as cytoskeletal dynamics, cell migration and cell cycle. Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers (PubMed:8910519, PubMed:9121475, PubMed:31570889). Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis (PubMed:16236794, PubMed:12900402). Plays an essential role in cleavage furrow formation. Required for the apical junction formation of keratinocyte cell-cell adhesion (PubMed:20974804, PubMed:23940119). Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly (PubMed:19934221). The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization (PubMed:20937854). Regulates KCNA2 potassium channel activity by reducing its location at the cell surface in response to CHRM1 activation; promotes KCNA2 endocytosis (PubMed:9635436, PubMed:19403695). Acts as an allosteric activator of guanine nucleotide exchange factor ECT2 by binding in its activated GTP-bound form to the PH domain of ECT2 which stimulates the release of PH inhibition and promotes the binding of substrate RHOA to the ECT2 catalytic center (PubMed:31888991). May be an activator of PLCE1 (PubMed:16103226). In neurons, involved in the inhibition of the initial spine growth. Upon activation by CaMKII, modulates dendritic spine structural plasticity by relaying CaMKII transient activation to synapse-specific, long-term signaling (By similarity). Acts as a regulator of platelet alpha-granule release during activation and aggregation of platelets (By similarity)

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