ARHGDIA

Last updated
ARHGDIA
Protein ARHGDIA PDB 1ajw.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases ARHGDIA , GDIA1, HEL-S-47e, NPHS8, RHOGDI, RHOGDI-1, Rho GDP dissociation inhibitor alpha
External IDs OMIM: 601925 MGI: 2178103 HomoloGene: 908 GeneCards: ARHGDIA
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_133796
NM_001363425

RefSeq (protein)

NP_598557
NP_001350354

Location (UCSC) Chr 17: 81.87 – 81.87 Mb Chr 11: 120.47 – 120.47 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Rho GDP-dissociation inhibitor 1 is a protein that in humans is encoded by the ARHGDIA gene. [5] [6]

Interactions

ARHGDIA has been shown to interact with:

Related Research Articles

GTPases are a large family of hydrolase enzymes that bind to the nucleotide guanosine triphosphate (GTP) and hydrolyze it to guanosine diphosphate (GDP). The GTP binding and hydrolysis takes place in the highly conserved P-loop "G domain", a protein domain common to many GTPases.

Small GTPases, also known as small G-proteins, are a family of hydrolase enzymes that can bind and hydrolyze guanosine triphosphate (GTP). They are a type of G-protein found in the cytosol that are homologous to the alpha subunit of heterotrimeric G-proteins, but unlike the alpha subunit of G proteins, a small GTPase can function independently as a hydrolase enzyme to bind to and hydrolyze a guanosine triphosphate (GTP) to form guanosine diphosphate (GDP). The best-known members are the Ras GTPases and hence they are sometimes called Ras subfamily GTPases.

The Rab family of proteins is a member of the Ras superfamily of small G proteins. Approximately 70 types of Rabs have now been identified in humans. Rab proteins generally possess a GTPase fold, which consists of a six-stranded beta sheet which is flanked by five alpha helices. Rab GTPases regulate many steps of membrane trafficking, including vesicle formation, vesicle movement along actin and tubulin networks, and membrane fusion. These processes make up the route through which cell surface proteins are trafficked from the Golgi to the plasma membrane and are recycled. Surface protein recycling returns proteins to the surface whose function involves carrying another protein or substance inside the cell, such as the transferrin receptor, or serves as a means of regulating the number of a certain type of protein molecules on the surface.

<span class="mw-page-title-main">Guanine nucleotide exchange factor</span> Proteins which remove GDP from GTPases

Guanine nucleotide exchange factors (GEFs) are proteins or protein domains that activate monomeric GTPases by stimulating the release of guanosine diphosphate (GDP) to allow binding of guanosine triphosphate (GTP). A variety of unrelated structural domains have been shown to exhibit guanine nucleotide exchange activity. Some GEFs can activate multiple GTPases while others are specific to a single GTPase.

<span class="mw-page-title-main">Guanosine nucleotide dissociation inhibitor</span>

In molecular biology, the Guanosine dissociation inhibitors (GDIs) constitute a family of small GTPases that serve a regulatory role in vesicular membrane traffic. GDIs bind to the GDP-bound form of Rho and Rab small GTPases and not only prevent exchange, but also prevent the small GTPase from localizing at the membrane, which is their place of action. This inhibition can be removed by the action of a GDI displacement factor. GDIs also inhibit cdc42 by binding to its tail and preventing its insertion into membranes; hence it cannot trigger WASPs and cannot lead to nucleation of F-actin.

The Rho family of GTPases is a family of small signaling G proteins, and is a subfamily of the Ras superfamily. The members of the Rho GTPase family have been shown to regulate many aspects of intracellular actin dynamics, and are found in all eukaryotic kingdoms, including yeasts and some plants. Three members of the family have been studied in detail: Cdc42, Rac1, and RhoA. All G proteins are "molecular switches", and Rho proteins play a role in organelle development, cytoskeletal dynamics, cell movement, and other common cellular functions.

<span class="mw-page-title-main">CDC42</span> Protein-coding gene in the species Homo sapiens

Cell division control protein 42 homolog, also known as Cdc42, is a protein involved in regulation of the cell cycle. It was originally identified in S. cerevisiae (yeast) as a mediator of cell division, and is now known to influence a variety of signaling events and cellular processes in a variety of organisms from yeast to mammals.

<span class="mw-page-title-main">RHOB</span>

Ras homolog gene family, member B, also known as RHOB, is a protein which in humans is encoded by the RHOB gene.

<span class="mw-page-title-main">RAC1</span> Protein-coding gene in the species Homo sapiens

Rac1, also known as Ras-related C3 botulinum toxin substrate 1, is a protein found in human cells. It is encoded by the RAC1 gene. This gene can produce a variety of alternatively spliced versions of the Rac1 protein, which appear to carry out different functions.

<span class="mw-page-title-main">Transforming protein RhoA</span> Protein-coding gene in the species Homo sapiens

Transforming protein RhoA, also known as Ras homolog family member A (RhoA), is a small GTPase protein in the Rho family of GTPases that in humans is encoded by the RHOA gene. While the effects of RhoA activity are not all well known, it is primarily associated with cytoskeleton regulation, mostly actin stress fibers formation and actomyosin contractility. It acts upon several effectors. Among them, ROCK1 and DIAPH1 are the best described. RhoA, and the other Rho GTPases, are part of a larger family of related proteins known as the Ras superfamily, a family of proteins involved in the regulation and timing of cell division. RhoA is one of the oldest Rho GTPases, with homologues present in the genomes since 1.5 billion years. As a consequence, RhoA is somehow involved in many cellular processes which emerged throughout evolution. RhoA specifically is regarded as a prominent regulatory factor in other functions such as the regulation of cytoskeletal dynamics, transcription, cell cycle progression and cell transformation.

<span class="mw-page-title-main">GDI1</span> Protein-coding gene in the species Homo sapiens

Rab GDP dissociation inhibitor alpha is a protein that in humans is encoded by the GDI1 gene.

<span class="mw-page-title-main">RHO protein GDP dissociation inhibitor</span>

RHO protein GDP dissociation inhibitor of Rho proteins, regulates GDP/GTP exchange.

<span class="mw-page-title-main">RAC2</span>

Rac2 is a small signaling G protein, and is a member of the Rac subfamily of the family Rho family of GTPases. It is encoded by the gene RAC2.

<span class="mw-page-title-main">ARHGDIB</span> Protein-coding gene in the species Homo sapiens

Rho GDP-dissociation inhibitor 2 is a protein that in humans is encoded by the ARHGDIB gene. Aliases of this gene include RhoGDI2, GDID4, Rho GDI 2, and others.

<span class="mw-page-title-main">RhoG</span>

RhoG is a small monomeric GTP-binding protein, and is an important component of many intracellular signalling pathways. It is a member of the Rac subfamily of the Rho family of small G proteins and is encoded by the gene RHOG.

<span class="mw-page-title-main">GDI2</span>

Rab GDP dissociation inhibitor beta is a protein that in humans is encoded by the GDI2 gene.

<span class="mw-page-title-main">ARHGDIG</span>

Rho GDP-dissociation inhibitor 3 is a protein that in humans is encoded by the ARHGDIG gene.

<span class="mw-page-title-main">RhoH</span>

RhoH is a small signaling G protein, and is a member of the Rac subfamily of the family Rho family of GTPases. It is encoded by the gene RHOH.

TCL is a small signaling G protein, and is a member of the Rho family of GTPases.,.

<span class="mw-page-title-main">GoLoco motif</span> Protein structural motif

GoLoco motif is a protein structural motif.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000141522 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000025132 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Wagner T, Tommerup N, Wirth J, Leffers H, Zimmer J, Back E, Weissenbach J, Scherer G (July 1997). "A somatic cell hybrid panel for distal 17q: GDIA1 maps to 17q25.3". Cytogenet Cell Genet. 76 (3–4): 172–5. doi:10.1159/000134538. PMID   9186513.
  6. "Entrez Gene: ARHGDIA Rho GDP dissociation inhibitor (GDI) alpha".
  7. 1 2 3 Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMC   1847948 . PMID   17353931.
  8. 1 2 3 4 Gorvel JP, Chang TC, Boretto J, Azuma T, Chavrier P (January 1998). "Differential properties of D4/LyGDI versus RhoGDI: phosphorylation and rho GTPase selectivity". FEBS Lett. 422 (2): 269–73. doi:10.1016/s0014-5793(98)00020-9. PMID   9490022. S2CID   10817327.
  9. 1 2 3 4 Fauré J, Dagher MC (May 2001). "Interactions between Rho GTPases and Rho GDP dissociation inhibitor (Rho-GDI)". Biochimie. 83 (5): 409–14. doi:10.1016/s0300-9084(01)01263-9. PMID   11368848.
  10. Grizot S, Fauré J, Fieschi F, Vignais PV, Dagher MC, Pebay-Peyroula E (August 2001). "Crystal structure of the Rac1-RhoGDI complex involved in nadph oxidase activation". Biochemistry. 40 (34): 10007–13. doi:10.1021/bi010288k. PMID   11513578.
  11. Lian LY, Barsukov I, Golovanov AP, Hawkins DI, Badii R, Sze KH, Keep NH, Bokoch GM, Roberts GC (January 2000). "Mapping the binding site for the GTP-binding protein Rac-1 on its inhibitor RhoGDI-1". Structure. 8 (1): 47–55. doi: 10.1016/s0969-2126(00)00080-0 . PMID   10673424.
  12. Di-Poï N, Fauré J, Grizot S, Molnár G, Pick E, Dagher MC (August 2001). "Mechanism of NADPH oxidase activation by the Rac/Rho-GDI complex". Biochemistry. 40 (34): 10014–22. doi:10.1021/bi010289c. PMID   11513579.
  13. Gajate C, Mollinedo F (March 2005). "Cytoskeleton-mediated death receptor and ligand concentration in lipid rafts forms apoptosis-promoting clusters in cancer chemotherapy". J. Biol. Chem. 280 (12): 11641–7. doi: 10.1074/jbc.M411781200 . PMID   15659383.
  14. Michaelson D, Silletti J, Murphy G, D'Eustachio P, Rush M, Philips MR (January 2001). "Differential localization of Rho GTPases in live cells: regulation by hypervariable regions and RhoGDI binding". J. Cell Biol. 152 (1): 111–26. doi:10.1083/jcb.152.1.111. PMC   2193662 . PMID   11149925.
  15. Li X, Bu X, Lu B, Avraham H, Flavell RA, Lim B (February 2002). "The hematopoiesis-specific GTP-binding protein RhoH is GTPase deficient and modulates activities of other Rho GTPases by an inhibitory function". Mol. Cell. Biol. 22 (4): 1158–71. doi:10.1128/mcb.22.4.1158-1171.2002. PMC   134637 . PMID   11809807.

Further reading