پروتئین مبدل RhoA

RHOA
ساختارهای موجود
PDB	جستجوی هم‌ساخت‌شناسی: PDBe RCSB
فهرست شناسه‌های PDB
	5BWM, 1A2B, 1CC0, 1CXZ, 1DPF, 1FTN, 1KMQ, 1LB1, 1OW3, 1S1C, 1TX4, 1X86, 1XCG, 2RGN, 3KZ1, 3LW8, 3LWN, 3LXR, 3MSX, 3T06, 4D0N, 4XH9, 4XSG, 4XSH, 4XOI, 5A0F, 5FR2, 5FR1, 5JCP, 5C2K, 5C4M, 5HPY
معین‌کننده‌ها
نام‌های دیگر	RHOA, ARH12, ARHA, RHO12, RHOH12, ras homolog family member A, EDFAOB
شناسه‌های بیرونی	OMIM: 165390 MGI: 1096342 HomoloGene: 68986 GeneCards: RHOA
موقعیت ژن (موش)
کروموزوم	کروموزوم ۹ (موش)
پایان	108,215,133 bp
الگوی گسترش RNA
	; ; ; ;
	More reference expression data
هستی‌شناسی ژن
عملکرد ملکولی	• nucleotide binding; • myosin binding; • GTP binding; • GO:0001948، GO:0016582 پیوند پروتئینی; • GO:0006184 GTPase activity; • GDP binding; • protein kinase binding; • protein domain specific binding; • Rho GDP-dissociation inhibitor binding;
ترکیبات سلولی	• سیتوپلاسم; • ریزکیسه; • سیتوزول; • اندوزوم; • cell projection; • endoplasmic reticulum membrane; • membrane; • focal adhesion; • extrinsic component of cytoplasmic side of plasma membrane; • پوسته یاخته; • پیوند میان‌یاخته‌ای; • cell cortex; • midbody; • cleavage furrow; • اسکلت سلولی; • apical junction complex; • extracellular exosome; • cell periphery; • پای‌لایه; • secretory granule membrane; • ficolin-1-rich granule membrane; • هسته یاخته; • آسه; • cell division site; • ruffle membrane; • dendritic spine; • intracellular membrane-bounded organelle; • postsynapse; • glutamatergic synapse; • intracellular anatomical structure;
فرایند زیستی	• actin cytoskeleton reorganization; • ossification involved in bone maturation; • apolipoprotein A-I-mediated signaling pathway; • regulation of cell migration; • negative chemotaxis; • regulation of actin cytoskeleton organization; • cleavage furrow formation; • substantia nigra development; • ephrin receptor signaling pathway; • endothelial tube lumen extension; • Roundabout signaling pathway; • positive regulation of axonogenesis; • stress fiber assembly; • positive regulation of lipase activity; • regulation of osteoblast proliferation; • تقسیم یاخته; • positive regulation of cytokinesis; • platelet activation; • negative regulation of cell migration involved in sprouting angiogenesis; • positive regulation of protein serine/threonine kinase activity; • mitotic cleavage furrow formation; • mitotic spindle assembly; • negative regulation of axonogenesis; • vascular endothelial growth factor receptor signaling pathway; • skeletal muscle satellite cell migration; • trabecula morphogenesis; • positive regulation of neuron differentiation; • Rho protein signal transduction; • positive regulation of I-kappaB kinase/NF-kappaB signaling; • چرخه یاخته‌ای; • GO:0022415 viral process; • regulation of small GTPase mediated signal transduction; • transforming growth factor beta receptor signaling pathway; • کوچ یاخته; • apical junction assembly; • wound healing, spreading of cells; • endothelial cell migration; • positive regulation of stress fiber assembly; • actin cytoskeleton organization; • phosphatidylinositol-mediated signaling; • small GTPase mediated signal transduction; • regulation of cell motility; • Wnt signaling pathway, planar cell polarity pathway; • protein deubiquitination; • neutrophil degranulation; • GO:0000767 cell morphogenesis; • response to hypoxia; • angiotensin-mediated vasoconstriction involved in regulation of systemic arterial blood pressure; • alpha-beta T cell lineage commitment; • regulation of systemic arterial blood pressure by endothelin; • GO:0044324، GO:0003256، GO:1901213، GO:0046019، GO:0046020، GO:1900094، GO:0061216، GO:0060994، GO:1902064، GO:0003258، GO:0072212 regulation of transcription by RNA polymerase II; • cytoskeleton organization; • actin filament organization; • چسبندگی سلولی; • cell-matrix adhesion; • G protein-coupled receptor signaling pathway; • skeletal muscle tissue development; • regulation of actin polymerization or depolymerization; • regulation of cell shape; • response to mechanical stimulus; • response to glucose; • negative regulation of cell-substrate adhesion; • regulation of neuron projection development; • negative regulation of neuron projection development; • cerebral cortex cell migration; • forebrain radial glial cell differentiation; • دگرگونی یاخته‌; • positive regulation of cell growth; • positive regulation of cell migration; • androgen receptor signaling pathway; • positive regulation of actin filament polymerization; • establishment or maintenance of actin cytoskeleton polarity; • stress-activated protein kinase signaling cascade; • negative regulation of intracellular steroid hormone receptor signaling pathway; • cell junction assembly; • odontogenesis; • negative regulation of I-kappaB kinase/NF-kappaB signaling; • response to amino acid; • positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; • beta selection; • GO:1904089 negative regulation of neuron apoptotic process; • positive regulation of neuron apoptotic process; • establishment of epithelial cell apical/basal polarity; • response to ethanol; • negative regulation of neuron differentiation; • positive regulation of translation; • positive regulation of cell adhesion; • negative regulation of cell size; • positive regulation of vasoconstriction; • positive regulation of smooth muscle contraction; • GTP metabolic process; • positive regulation of alpha-beta T cell differentiation; • neuron projection morphogenesis; • regulation of dendrite development; • actin filament bundle assembly; • response to glucocorticoid; • regulation of focal adhesion assembly; • regulation of calcium ion transport; • negative regulation of cell death; • regulation of microtubule cytoskeleton organization; • cellular response to lipopolysaccharide; • cellular response to cytokine stimulus; • positive regulation of podosome assembly; • negative regulation of oxidative phosphorylation; • positive regulation of NIK/NF-kappaB signaling; • negative regulation of reactive oxygen species biosynthetic process; • positive regulation of vascular associated smooth muscle contraction; • positive regulation of leukocyte adhesion to vascular endothelial cell; • regulation of modification of synaptic structure; • regulation of modification of postsynaptic actin cytoskeleton; • cellular response to chemokine; • regulation of neural precursor cell proliferation; • positive regulation of T cell migration;
	منابع: آمیگو / کوئیک‌گو
هم‌ساخت‌شناسی
	387
	11848
	ENSG00000067560
	ENSMUSG00000007815
	P61586
	Q9QUI0
	NM_001313943، NM_001313944، NM_001313945، NM_001313946، NM_001313947، NM_001664 NM_001313941، NM_001313943، NM_001313944، NM_001313945، NM_001313946، NM_001313947، NM_001664
	NM_001313961، NM_001313962 NM_016802، NM_001313961، NM_001313962
	NP_001300872، NP_001300873، NP_001300874، NP_001300875، NP_001300876، NP_001655 NP_001300870، NP_001300872، NP_001300873، NP_001300874، NP_001300875، NP_001300876، NP_001655; NP_001655.1، XP_011531997.1 NP_001300870.1، NP_001655.1، XP_011531997.1
	NP_001300891، NP_058082 NP_001300890، NP_001300891، NP_058082
	ویکی‌داده
مشاهده/ویرایش انسان	مشاهده/ویرایش موش

پروتئین مبدل RhoA (انگلیسی: Transforming protein RhoA) یک پروتئین است که در انسان توسط ژن «RHOA» کُدگذاری می‌شود.^[۴] این پروتئین بر روی چندین مولکول مهم دیگر از جمله آراوسی‌کی۱^[۵]^[۶] و ITPR1^[۷]^[۸] اثر می‌گذارد و یکی از قدیمی‌ترین جی‌پروتئین‌های شناخته شده‌است که هومولوگ‌های آن در ژنوم از حدود ۱٫۵ میلیارد سال پیش موجود بوده‌اند.

ژن «RHOA» بر روی بازوی کوتاه کروموزوم ۳ واقع شده‌است و از ۴ اگزون تشکیل شده‌است.^[۹] پروتئین حاصل‌شده در سازمان‌دهی اکتین، انقباض میوزین، حفظ چرخه سلولی، پلاریزاسیون مورفولوژیکی سلولی، تکامل سلولی و کنترل رونویسی نقش دارد.

اهمیت بالینی

با توجه به اینکه بیان بیش از حد ژن «RHOA» در بسیاری از بدخیمی‌ها یافت مشاهده شده‌است، فعالیت RhoA به دلیل دخالت قابل توجه آن در مسیرهای پیام‌رسانی سرطان، ممکن است در بروز برخی بدخیمی‌ها از جمله سرطان پروستات^[۱۰] و سرطان معده^[۱۱] دخالت داشته باشد. از این ژن ممکن است بتوان در آینده برای ژن‌درمانی سرطان^[۱۲] به‌ویژه در درمان لوسمی مزمن مغز استخوان^[۱۳] و درمان سرطان پستان^[۱۴] استفاده کرد.

همچنین برخی پژوهش‌ها نشان داده‌اند که این پروتئین ممکن از اهداف درمان دارویی آسم^[۱۵] و دیابت^[۱۶] در آینده باشند.

منابع

↑ ^۱٫۰ ^۱٫۱ ^۱٫۲ GRCm38: Ensembl release 89: ENSMUSG00000007815 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Kiss C, Li J, Szeles A, Gizatullin RZ, Kashuba VI, Lushnikova T, et al. (1997). "Assignment of the ARHA and GPX1 genes to human chromosome bands 3p21.3 by in situ hybridization and with somatic cell hybrids". Cytogenetics and Cell Genetics. 79 (3–4): 228–30. doi:10.1159/000134729. PMID 9605859.
↑ Leung T, Chen XQ, Manser E, Lim L (October 1996). "The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton". Molecular and Cellular Biology. 16 (10): 5313–27. doi:10.1128/mcb.16.10.5313. PMC 231530. PMID 8816443.
↑ Fujisawa K, Fujita A, Ishizaki T, Saito Y, Narumiya S (September 1996). "Identification of the Rho-binding domain of p160ROCK, a Rho-associated coiled-coil containing protein kinase". The Journal of Biological Chemistry. 271 (38): 23022–8. doi:10.1074/jbc.271.38.23022. PMID 8798490.
↑ Riento K, Guasch RM, Garg R, Jin B, Ridley AJ (June 2003). "RhoE binds to ROCK I and inhibits downstream signaling". Molecular and Cellular Biology. 23 (12): 4219–29. doi:10.1128/mcb.23.12.4219-4229.2003. PMC 156133. PMID 12773565.
↑ Mehta D, Ahmmed GU, Paria BC, Holinstat M, Voyno-Yasenetskaya T, Tiruppathi C, et al. (August 2003). "RhoA interaction with inositol 1,4,5-trisphosphate receptor and transient receptor potential channel-1 regulates Ca2+ entry. Role in signaling increased endothelial permeability". The Journal of Biological Chemistry. 278 (35): 33492–500. doi:10.1074/jbc.M302401200. PMID 12766172.
↑ Oliyarnyk O, Renner W, Paulweber B, Wascher TC (April 2005). "Interindividual differences of response to statin treatment cannot be explained by variations of the human gene for RhoA". Biochemical Genetics. 43 (3–4): 143–8. doi:10.1007/s10528-005-1507-0. PMID 15932062. S2CID 11149758.
↑ Schmidt LJ, Duncan K, Yadav N, Regan KM, Verone AR, Lohse CM, et al. (May 2012). "RhoA as a mediator of clinically relevant androgen action in prostate cancer cells". Molecular Endocrinology. 26 (5): 716–35. doi:10.1210/me.2011-1130. PMC 3355556. PMID 22456196.
↑ Zhang S, Tang Q, Xu F, Xue Y, Zhen Z, Deng Y, et al. (April 2009). "RhoA regulates G1-S progression of gastric cancer cells by modulation of multiple INK4 family tumor suppressors". Molecular Cancer Research. 7 (4): 570–80. doi:10.1158/1541-7786.MCR-08-0248. PMID 19372585.
↑ Doublier S, Riganti C, Voena C, Costamagna C, Aldieri E, Pescarmona G, et al. (October 2008). "RhoA silencing reverts the resistance to doxorubicin in human colon cancer cells". Molecular Cancer Research. 6 (10): 1607–20. doi:10.1158/1541-7786.MCR-08-0251. PMID 18922976.
↑ Molli PR, Pradhan MB, Advani SH, Naik NR (March 2012). "RhoA: a therapeutic target for chronic myeloid leukemia". Molecular Cancer. 11 (1): 16. doi:10.1186/1476-4598-11-16. PMC 3353160. PMID 22443473.
↑ Shang X, Marchioni F, Sipes N, Evelyn CR, Jerabek-Willemsen M, Duhr S, et al. (June 2012). "Rational design of small molecule inhibitors targeting RhoA subfamily Rho GTPases". Chemistry & Biology. 19 (6): 699–710. doi:10.1016/j.chembiol.2012.05.009. PMC 3383629. PMID 22726684.
↑ Kume H (2008). "RhoA/Rho-kinase as a therapeutic target in asthma". Current Medicinal Chemistry. 15 (27): 2876–85. doi:10.2174/092986708786242831. PMID 18991642.
↑ Zhou H, Li YJ (September 2010). "RhoA/Rho kinase: a novel therapeutic target in diabetic complications". Chinese Medical Journal. 123 (17): 2461–6. PMID 21034566.

مشارکت‌کنندگان ویکی‌پدیا. «Transforming protein RhoA». در دانشنامهٔ ویکی‌پدیای انگلیسی، بازبینی‌شده در ۱۷ اکتبر ۲۰۲۲.

پیوند به بیرون

rhoA Protein در سرعنوان‌های موضوعی پزشکی (MeSH) در کتابخانهٔ ملی پزشکی ایالات متحدهٔ آمریکا
خلاصه‌ای از اطلاعات ساختاری موجود در بانک داده پروتئین برای یونی‌پروت: P61586 (Human Transforming protein RhoA) در PDBe-KB.
خلاصه‌ای از اطلاعات ساختاری موجود در بانک داده پروتئین برای یونی‌پروت: Q9QUI0 (Mouse Transforming protein RhoA) در PDBe-KB.

برای مطالعهٔ بیشتر

Ramakers GJ (April 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. S2CID 13941716.
Chang ZF, Lee HH (March 2006). "RhoA signaling in phorbol ester-induced apoptosis". Journal of Biomedical Science. 13 (2): 173–80. doi:10.1007/s11373-005-9056-4. PMID 16496227.

این یک مقالهٔ خرد زیست‌شناسی مولکولی است. می‌توانید با گسترش آن به ویکی‌پدیا کمک کنید.

[refGRCm38Ensembl-1] ۱٫۰ ^۱٫۱ ^۱٫۲ GRCm38: Ensembl release 89: ENSMUSG00000007815 - Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[3] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid_9605859-4] Kiss C, Li J, Szeles A, Gizatullin RZ, Kashuba VI, Lushnikova T, et al. (1997). "Assignment of the ARHA and GPX1 genes to human chromosome bands 3p21.3 by in situ hybridization and with somatic cell hybrids". Cytogenetics and Cell Genetics. 79 (3–4): 228–30. doi:10.1159/000134729. PMID 9605859.

[pmid_8816443-5] Leung T, Chen XQ, Manser E, Lim L (October 1996). "The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton". Molecular and Cellular Biology. 16 (10): 5313–27. doi:10.1128/mcb.16.10.5313. PMC 231530. PMID 8816443.

[pmid_8798490-6] Fujisawa K, Fujita A, Ishizaki T, Saito Y, Narumiya S (September 1996). "Identification of the Rho-binding domain of p160ROCK, a Rho-associated coiled-coil containing protein kinase". The Journal of Biological Chemistry. 271 (38): 23022–8. doi:10.1074/jbc.271.38.23022. PMID 8798490.

[pmid12773565-7] Riento K, Guasch RM, Garg R, Jin B, Ridley AJ (June 2003). "RhoE binds to ROCK I and inhibits downstream signaling". Molecular and Cellular Biology. 23 (12): 4219–29. doi:10.1128/mcb.23.12.4219-4229.2003. PMC 156133. PMID 12773565.

[pmid12766172-8] Mehta D, Ahmmed GU, Paria BC, Holinstat M, Voyno-Yasenetskaya T, Tiruppathi C, et al. (August 2003). "RhoA interaction with inositol 1,4,5-trisphosphate receptor and transient receptor potential channel-1 regulates Ca2+ entry. Role in signaling increased endothelial permeability". The Journal of Biological Chemistry. 278 (35): 33492–500. doi:10.1074/jbc.M302401200. PMID 12766172.

[pmid_15932062-9] Oliyarnyk O, Renner W, Paulweber B, Wascher TC (April 2005). "Interindividual differences of response to statin treatment cannot be explained by variations of the human gene for RhoA". Biochemical Genetics. 43 (3–4): 143–8. doi:10.1007/s10528-005-1507-0. PMID 15932062. S2CID 11149758.

[pmid22456196-10] Schmidt LJ, Duncan K, Yadav N, Regan KM, Verone AR, Lohse CM, et al. (May 2012). "RhoA as a mediator of clinically relevant androgen action in prostate cancer cells". Molecular Endocrinology. 26 (5): 716–35. doi:10.1210/me.2011-1130. PMC 3355556. PMID 22456196.

[pmid19372585-11] Zhang S, Tang Q, Xu F, Xue Y, Zhen Z, Deng Y, et al. (April 2009). "RhoA regulates G1-S progression of gastric cancer cells by modulation of multiple INK4 family tumor suppressors". Molecular Cancer Research. 7 (4): 570–80. doi:10.1158/1541-7786.MCR-08-0248. PMID 19372585.

[pmid18922976-12] Doublier S, Riganti C, Voena C, Costamagna C, Aldieri E, Pescarmona G, et al. (October 2008). "RhoA silencing reverts the resistance to doxorubicin in human colon cancer cells". Molecular Cancer Research. 6 (10): 1607–20. doi:10.1158/1541-7786.MCR-08-0251. PMID 18922976.

[pmid22443473-13] Molli PR, Pradhan MB, Advani SH, Naik NR (March 2012). "RhoA: a therapeutic target for chronic myeloid leukemia". Molecular Cancer. 11 (1): 16. doi:10.1186/1476-4598-11-16. PMC 3353160. PMID 22443473.

[pmid22726684-14] Shang X, Marchioni F, Sipes N, Evelyn CR, Jerabek-Willemsen M, Duhr S, et al. (June 2012). "Rational design of small molecule inhibitors targeting RhoA subfamily Rho GTPases". Chemistry & Biology. 19 (6): 699–710. doi:10.1016/j.chembiol.2012.05.009. PMC 3383629. PMID 22726684.

[pmid18991642-15] Kume H (2008). "RhoA/Rho-kinase as a therapeutic target in asthma". Current Medicinal Chemistry. 15 (27): 2876–85. doi:10.2174/092986708786242831. PMID 18991642.

[pmid21034566-16] Zhou H, Li YJ (September 2010). "RhoA/Rho kinase: a novel therapeutic target in diabetic complications". Chinese Medical Journal. 123 (17): 2461–6. PMID 21034566.

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