RAC1

RAC1
Dostupne strukture
PDB	Pretraga ortologa: PDBe RCSB
Spisak PDB ID kodova
	1E96, 1FOE, 1G4U, 1HE1, 1HH4, 1I4D, 1I4L, 1I4T, 1MH1, 1RYF, 1RYH, 2FJU, 2H7V, 2NZ8, 2P2L, 2RMK, 2VRW, 2WKP, 2WKQ, 2WKR, 2YIN, 3B13, 3BJI, 3RYT, 3SBD, 3SBE, 3SU8, 3SUA, 3TH5, 4GZL, 4GZM, 4YON, 5FI0
Identifikatori
Aliasi	RAC1
Vanjski ID-jevi	OMIM: 602048 MGI: 97845 HomoloGene: 69035 GeneCards: RAC1
Lokacija gena (čovjek)
Hrom.	Hromosom 7 (čovjek)
Kraj	6,403,967 bp
Lokacija gena (miš)
Hrom.	Hromosom 5 (miš)
Kraj	143,513,791 bp
Obrazac RNK ekspresije
	; ;
	Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija	• histone deacetylase binding; • Rho GDP-dissociation inhibitor binding; • GTP-dependent protein binding; • GO:0006184 GTPase activity; • vezivanje enzima; • GO:0001948, GO:0016582 vezivanje za proteine; • thioesterase binding; • protein kinase binding; • nucleotide binding; • GTP binding; • protein serine/threonine kinase activity; • GO:0032403 protein-containing complex binding; • phosphatidylinositol-4,5-bisphosphate 3-kinase activity; • ATPase binding;
Ćelijska komponenta	• citoplazma; • citosol; • membrana; • focal adhesion; • Melanosom; • ruffle membrane; • trans-Golđijeva mreža; • jedro; • projekcija ćelije; • extrinsic component of plasma membrane; • Egzosom; • lamellipodium; • early endosome membrane; • ćelijska membrana; • Mikronit; • cytoplasmic ribonucleoprotein granule; • endoplasmic reticulum membrane; • Golđijeva membrana; • phagocytic cup; • GO:0016023 citoplazmatska vezikula; • GO:0005578 Vanćelijski matriks; • secretory granule membrane; • dendritična kičma; • recycling endosome membrane; • postsynapse; • glutamatergic synapse; • ficolin-1-rich granule membrane;
Biološki proces	• positive regulation of Rho protein signal transduction; • regulation of respiratory burst; • non-canonical Wnt signaling pathway; • positive regulation of protein phosphorylation; • positive regulation of actin filament polymerization; • regulation of neuron maturation; • negative regulation of receptor-mediated endocytosis; • platelet activation; • Fc-epsilon receptor signaling pathway; • cellular response to mechanical stimulus; • phagocytosis, engulfment; • vascular endothelial growth factor receptor signaling pathway; • substrate adhesion-dependent cell spreading; • Ćelijska proliferacija; • ruffle assembly; • lamellipodium assembly; • dopaminergic neuron differentiation; • cell-cell junction organization; • Fc-gamma receptor signaling pathway involved in phagocytosis; • ruffle organization; • actin filament organization; • cell motility; • anatomical structure morphogenesis; • bone resorption; • response to wounding; • protein localization to plasma membrane; • inflammatory response; • regulation of small GTPase mediated signal transduction; • positive regulation of cell-substrate adhesion; • G protein-coupled receptor signaling pathway; • neuron projection morphogenesis; • epithelial cell morphogenesis; • dendrite morphogenesis; • regulation of hydrogen peroxide metabolic process; • engulfment of apoptotic cell; • dendrite development; • auditory receptor cell morphogenesis; • hyperosmotic response; • cerebral cortex GABAergic interneuron development; • Hemotaksija; • positive regulation of DNA replication; • actin filament polymerization; • Ćelijska adhezija; • negative regulation of interleukin-23 production; • homeostasis of number of cells within a tissue; • cell-matrix adhesion; • localization within membrane; • actin cytoskeleton organization; • regulation of cell size; • anatomical structure arrangement; • GO:0007243 intracellular signal transduction; • regulation of cell migration; • Endocitoza; • ephrin receptor signaling pathway; • T cell costimulation; • Koagulacija (krv); • GO:0019049, GO:0030683 mitigation of host defenses by virus; • synaptic transmission, GABAergic; • mast cell chemotaxis; • positive regulation of phosphatidylinositol 3-kinase activity; • positive regulation of substrate adhesion-dependent cell spreading; • embryonic olfactory bulb interneuron precursor migration; • cytoskeleton organization; • cochlea morphogenesis; • positive regulation of neutrophil chemotaxis; • positive regulation of apoptotic process; • regulation of cell morphogenesis; • positive regulation of focal adhesion assembly; • regulation of fibroblast migration; • positive regulation of lamellipodium assembly; • cerebral cortex radially oriented cell migration; • Ćelijska migracija; • semaphorin-plexin signaling pathway; • positive regulation of stress fiber assembly; • axon guidance; • small GTPase mediated signal transduction; • GO:0032320, GO:0032321, GO:0032855, GO:0043089, GO:0032854 positive regulation of GTPase activity; • Wnt signaling pathway, planar cell polarity pathway; • midbrain dopaminergic neuron differentiation; • neuron migration; • protein phosphorylation; • Rho protein signal transduction; • regulation of lamellipodium assembly; • Rac protein signal transduction; • cell projection assembly; • positive regulation of microtubule polymerization; • neutrophil degranulation; • regulation of nitric oxide biosynthetic process; • phosphatidylinositol phosphate biosynthetic process; • hepatocyte growth factor receptor signaling pathway; • regulation of stress fiber assembly; • positive regulation of protein kinase B signaling; • motor neuron axon guidance; • regulation of neutrophil migration; • positive regulation of insulin secretion involved in cellular response to glucose stimulus;
	Izvori:Amigo / QuickGO
Ortolozi
	5879
	19353
	ENSG00000136238
	ENSMUSG00000001847
	P63000
	P63001
	NM_198829; NM_006908; NM_018890
	NM_009007; NM_001347530
	NP_008839; NP_061485
	NP_001334459; NP_033033
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Rac1, poznat i kao Ras-srodni C3 supstrat botulinum toksina 1, je protein koji se nalazi u ljudskim ćelijama. Kodiran je genom RAC1.^[5]^[6] Ovaj gen može proizvesti razne alternativna prerade verzija proteina Rac1, za koje se čini da imaju različite funkcije.^[7]

Funkcija

Rac1 je mal (~ 21 kDa) signalizirajući G protein (tačnije GTPaza) i član je potporodice Rac porodice porodice Rho GTPaza. Članovi ove superporodice reguliraju raznolik niz ćelijskih događaja, uključujući kontrolu GLUT4,^[8]^[9] translokaciju do unosa glukoze, rast ćelija, reorganizaciju citoskeleta, antimikrobnu citotoksičnost,^[10] i aktivaciju protein kinaza.^[11]

Rac1 je plejotropni regulator mnogih ćelijskih procesa, uključujući ćelijski ciklus, adheziju ćelijskih ćelija, pokretljivost (kroz aktinsku mrežu) i epitelnu diferencijaciju (predloženo da je neophodan za održavanje epidermnih matičnih ćelija).

Uloga u kanceru

Zajedno s drugom potporodicama, Rac i Rho proteina, imaj važnu regulatornu ulogu, posebno u pokretljivosti i rastu ćelija. Rac1 ima sveprisutnu tkivnu ekspresiju i podstiče pokretljivost ćelija stvaranjem lamelipodija.^[12] Da bi ćlije raka mogle rasti i napadati lokalna i udaljena tkiva, deregulacija pokretljivosti ćelija jedan je od glavnih događaja u invaziji i [metastaza|[metastaziranju]] ćelija karcinoma.^[13] Prekomjerna ekspresija konstitucijski aktivnog Rac1 V12 kod miševa uzrokovala je tumor koji se fenotipski ne razlikuje od ljudsog Kaposijevog sarkoma.^[14] Pokazalo se da aktivacijske ili dobitne funkcije mutacije Rac1 imaju aktivnu ulogu u promociji mezenhimskog tipa kretanja ćelija, potpomognutog proteinskim kompleksima NEDD9 i DOCK3.^[15] Takva abnormalna pokretljivost ćelija može rezultirati tranzicijom epitelnog mezenhima (EMT) – pokretačkim mehanizmom za metastaziranje tumora, kao i relapse tumora rezistentnog na lijekove.^[16]^[17]

Uloga u transportu glukoze

Rac1 se ispoljava u značajnim količinama u tkivima osjetljivim na insulin, kau što su masno tkivo i skeletni mišići. Ovdje Rac1 regulira translokaciju prijenosnika glukoze GLUT4 iz unutarćelijskih odjeljaka u plazmamembranu.^[9]^[18]^[19] U odgovoru na insulin, ovo omogućava ulazak glukoze u krv u ćeliji, radi smanjenja glukoze u krvi. U uvjetima gojaznosti i dijabetesa tipa 2, signalizacija Rac1 u skeletnim mišićima je disfunkcionalna, što sugerira da Rac1 doprinosi napredovanju bolesti.

Protein Rac1 je također neophodan za unos glukoze u skeletne mišiće aktivirane vježbanjem^[8]^[20] i istezanjem.^[21]

Klinički značaj

Aktivirajuće mutacije u Rac1 nedavno su otkrivene u velikim genomskim studijama koje uključuju melanom^[22]^[23]^[24] i plućni karcinom malih ćelija.^[25] Kao rezultat toga, Rac1 se smatra terapijskom metom za mnoge od ovih bolesti.^[26]

Nekoliko nedavnih studija također je koristilo ciljanu terapiju za suzbijanje rasta tumora, farmakoinhibicijom aktivnosti Rac1 u metastatskom melanomu i karcinomu jetre, kao i u ljudskom [[Rak dojke|karcinomu dojke.^[27]^[28]^[29]

Naprimjer, inhibicija puta ovisnog o Rac1 rezultirala je preokretom fenotipa tumorskih ćelija, što sugerira Rac1 kao prediktivni marker i terapijski cilj za rak dojke otporan na trastuzumab. Međutim, s obzirom na ulogu Rac1 u transportu glukoze , lijekovi koji inhibiraju Rac1 mogli bi biti štetni za homeostazu glukoze.

Dominantno negativan ili konstitutivno aktivno, klicne linije mutacije RAC1 uzrokuju različite fenotipove, koji su grupirani kao mentalna retardacija Tip 48.^[30] Većina mutacija uzrokuje mikrocefaliju, dok neke specifične promjene rezultiraju makrocefalijom.

Interakcije

Pokazalo se da RAC1 ima interakcije sa:

Reference

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^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000001847 - Ensembl, maj 2017
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^ Katoh H, Negishi M (Jul 2003). "RhoG activates Rac1 by direct interaction with the Dock180-binding protein Elmo". Nature. 424 (6947): 461–4. doi:10.1038/nature01817. PMID 12879077.
^ Seoh ML, Ng CH, Yong J, Lim L, Leung T (Mar 2003). "ArhGAP15, a novel human RacGAP protein with GTPase binding property". FEBS Letters. 539 (1–3): 131–7. doi:10.1016/S0014-5793(03)00213-8. PMID 12650940.
^ ^a ^b Noda Y, Takeya R, Ohno S, Naito S, Ito T, Sumimoto H (Feb 2001). "Human homologues of the Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C". Genes to Cells. 6 (2): 107–19. doi:10.1046/j.1365-2443.2001.00404.x. PMID 11260256.
^ Qiu RG, Abo A, Steven Martin G (Jun 2000). "A human homolog of the C. elegans polarity determinant Par-6 links Rac and Cdc42 to PKCzeta signaling and cell transformation". Current Biology. 10 (12): 697–707. doi:10.1016/S0960-9822(00)00535-2. PMID 10873802.
^ Zhao C, Ma H, Bossy-Wetzel E, Lipton SA, Zhang Z, Feng GS (Sep 2003). "GC-GAP, a Rho family GTPase-activating protein that interacts with signaling adapters Gab1 and Gab2". The Journal of Biological Chemistry. 278 (36): 34641–53. doi:10.1074/jbc.M304594200. PMID 12819203.
^ Moon SY, Zang H, Zheng Y (Feb 2003). "Characterization of a brain-specific Rho GTPase-activating protein, p200RhoGAP". The Journal of Biological Chemistry. 278 (6): 4151–9. doi:10.1074/jbc.M207789200. PMID 12454018.
^ Simon AR, Vikis HG, Stewart S, Fanburg BL, Cochran BH, Guan KL (Oct 2000). "Regulation of STAT3 by direct binding to the Rac1 GTPase". Science. 290 (5489): 144–7. doi:10.1126/science.290.5489.144. PMID 11021801.
^ Worthylake DK, Rossman KL, Sondek J (Dec 2000). "Crystal structure of Rac1 in complex with the guanine nucleotide exchange region of Tiam1". Nature. 408 (6813): 682–8. doi:10.1038/35047014. PMID 11130063.
^ Gao Y, Xing J, Streuli M, Leto TL, Zheng Y (Dec 2001). "Trp(56) of rac1 specifies interaction with a subset of guanine nucleotide exchange factors". The Journal of Biological Chemistry. 276 (50): 47530–41. doi:10.1074/jbc.M108865200. PMID 11595749.

Dopunska literatura

Benitah SA, Frye M, Glogauer M, Watt FM (Aug 2005). "Stem cell depletion through epidermal deletion of Rac1". Science. 309 (5736): 933–5. doi:10.1126/science.1113579. PMID 16081735.
Ramakers GJ (Apr 2002). "Rho proteins, mental retardation and the cellular basis of cognition". Trends in Neurosciences. 25 (4): 191–9. doi:10.1016/S0166-2236(00)02118-4. PMID 11998687.
Esufali S, Charames GS, Bapat B (Oct 2007). "Suppression of nuclear Wnt signaling leads to stabilization of Rac1 isoforms". FEBS Letters. 581 (25): 4850–6. doi:10.1016/j.febslet.2007.09.013 1457000 Provjerite vrijednost parametra |doi= (pomoć). PMID 17888911.

Vanjski linkovi

rac1 GTP-Binding Protein na US National Library of Medicine Medical Subject Headings (MeSH)
RAC1 Info with links in the Cell Migration Gateway Arhivirano 11. 12. 2014. na Wayback Machine

Šablon:GTPaze

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000136238 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000001847 - Ensembl, maj 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.

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[pmid9148763-50] Kitamura Y, Kitamura T, Sakaue H, Maeda T, Ueno H, Nishio S, Ohno S, Osada S, Sakaue M, Ogawa W, Kasuga M (Mar 1997). "Interaction of Nck-associated protein 1 with activated GTP-binding protein Rac". The Biochemical Journal. 322 (3): 873–8. doi:10.1042/bj3220873. PMC 1218269. PMID 9148763.

[pmid12879077-51] Katoh H, Negishi M (Jul 2003). "RhoG activates Rac1 by direct interaction with the Dock180-binding protein Elmo". Nature. 424 (6947): 461–4. doi:10.1038/nature01817. PMID 12879077.

[pmid12650940-52] Seoh ML, Ng CH, Yong J, Lim L, Leung T (Mar 2003). "ArhGAP15, a novel human RacGAP protein with GTPase binding property". FEBS Letters. 539 (1–3): 131–7. doi:10.1016/S0014-5793(03)00213-8. PMID 12650940.

[pmid11260256-53] Noda Y, Takeya R, Ohno S, Naito S, Ito T, Sumimoto H (Feb 2001). "Human homologues of the Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C". Genes to Cells. 6 (2): 107–19. doi:10.1046/j.1365-2443.2001.00404.x. PMID 11260256.

[pmid10873802-54] Qiu RG, Abo A, Steven Martin G (Jun 2000). "A human homolog of the C. elegans polarity determinant Par-6 links Rac and Cdc42 to PKCzeta signaling and cell transformation". Current Biology. 10 (12): 697–707. doi:10.1016/S0960-9822(00)00535-2. PMID 10873802.

[pmid12819203-55] Zhao C, Ma H, Bossy-Wetzel E, Lipton SA, Zhang Z, Feng GS (Sep 2003). "GC-GAP, a Rho family GTPase-activating protein that interacts with signaling adapters Gab1 and Gab2". The Journal of Biological Chemistry. 278 (36): 34641–53. doi:10.1074/jbc.M304594200. PMID 12819203.

[pmid12454018-56] Moon SY, Zang H, Zheng Y (Feb 2003). "Characterization of a brain-specific Rho GTPase-activating protein, p200RhoGAP". The Journal of Biological Chemistry. 278 (6): 4151–9. doi:10.1074/jbc.M207789200. PMID 12454018.

[pmid11021801-57] Simon AR, Vikis HG, Stewart S, Fanburg BL, Cochran BH, Guan KL (Oct 2000). "Regulation of STAT3 by direct binding to the Rac1 GTPase". Science. 290 (5489): 144–7. doi:10.1126/science.290.5489.144. PMID 11021801.

[pmid11130063-58] Worthylake DK, Rossman KL, Sondek J (Dec 2000). "Crystal structure of Rac1 in complex with the guanine nucleotide exchange region of Tiam1". Nature. 408 (6813): 682–8. doi:10.1038/35047014. PMID 11130063.

[pmid11595749-59] Gao Y, Xing J, Streuli M, Leto TL, Zheng Y (Dec 2001). "Trp(56) of rac1 specifies interaction with a subset of guanine nucleotide exchange factors". The Journal of Biological Chemistry. 276 (50): 47530–41. doi:10.1074/jbc.M108865200. PMID 11595749.

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