RhoC

From Wikipedia, the free encyclopedia

Ras homolog family member C

PDB rendering based on 1a2b.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1Z2C, 2GCN, 2GCO, 2GCP

Identifiers

Symbols

RHOC; ARH9; ARHC; H9; RHOH9

External IDs

OMIM: 165380 MGI: 106028 HomoloGene: 90945 GeneCards: RHOC Gene

Gene Ontology
Molecular function	• signal transducer activity • protein binding • GTP binding
Cellular component	• nucleus • cytosol • plasma membrane • cleavage furrow
Biological process	• small GTPase mediated signal transduction • axon guidance • positive regulation of I-kappaB kinase/NF-kappaB cascade • apical junction assembly • regulation of small GTPase mediated signal transduction
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
113.24 – 113.25 Mb

Chr 3:
104.79 – 104.79 Mb

PubMed search

RhoC (Ras homolog gene family, member C) is a small (~21 kDa) signaling G protein (more specifically a GTPase), and is a member of the Rac subfamily of the family Rho family of GTPases.^[1] It is encoded by the gene RHOC. ^[2]

Mechanism and function

It cycles between inactive GDP-bound and active GTP-bound states and function as molecular switches in signal transduction cascades. Rho proteins promote reorganization of the actin cytoskeleton and regulate cell shape and motility. RhoC can activate formins such as mDia1 and FMNL2 to remodel the cytoskelton.^[3]

It is prenylated at its C-terminus, and localizes to the cytoplasm and plasma membrane. It is thought to be important in cell locomotion. Overexpression of this gene is associated with tumor cell invasion and metastasis. RhoC-deficient mice can still develop tumors but these fail to metastasize, arguing that RhoC is essential for metastasis.^[4]

References

↑ Ridley A. (2006). "Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking". Trends Cell Biol 16 (10): 522–9. doi:10.1016/j.tcb.2006.08.006. PMID 16949823.
↑ "Entrez Gene: RHOC ras homolog gene family, member C".
↑ Kitzing TM, Wang Y, Pertz O, Copeland JW, Grosse R (April 2010). "Formin-like 2 drives amoeboid invasive cell motility downstream of RhoC". Oncogene 29 (16): 2441–8. doi:10.1038/onc.2009.515. PMID 20101212.
↑ Hakem A, Sanchez-Sweatman O, You-Ten A, Duncan G, Wakeham A, Khokha R, Mak TW (September 2005). "RhoC is dispensable for embryogenesis and tumor initiation but essential for metastasis". Genes Dev. 19 (17): 1974–9. doi:10.1101/gad.1310805. PMC 1199568. PMID 16107613.

Wheeler AP, Ridley AJ (2004). "Why three Rho proteins? RhoA, RhoB, RhoC, and cell motility.". Exp. Cell Res. 301 (1): 43–9. doi:10.1016/j.yexcr.2004.08.012. PMID 15501444.
Adamson P, Paterson HF, Hall A (1992). "Intracellular localization of the P21rho proteins.". J. Cell Biol. 119 (3): 617–27. doi:10.1083/jcb.119.3.617. PMC 2289677. PMID 1383236.
Chardin P, Madaule P, Tavitian A (1988). "Coding sequence of human rho cDNAs clone 6 and clone 9.". Nucleic Acids Res. 16 (6): 2717. doi:10.1093/nar/16.6.2717. PMC 336400. PMID 3283705.
Madaule P, Axel R (1985). "A novel ras-related gene family.". Cell 41 (1): 31–40. doi:10.1016/0092-8674(85)90058-3. PMID 3888408.
Reid T, Furuyashiki T, Ishizaki T, et al. (1996). "Rhotekin, a new putative target for Rho bearing homology to a serine/threonine kinase, PKN, and rhophilin in the rho-binding domain.". J. Biol. Chem. 271 (23): 13556–60. doi:10.1074/jbc.271.23.13556. PMID 8662891.
Maekawa M, Ishizaki T, Boku S, et al. (1999). "Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase.". Science 285 (5429): 895–8. doi:10.1126/science.285.5429.895. PMID 10436159.
Clark EA, Golub TR, Lander ES, Hynes RO (2000). "Genomic analysis of metastasis reveals an essential role for RhoC.". Nature 406 (6795): 532–5. doi:10.1038/35020106. PMID 10952316.
Diviani D, Soderling J, Scott JD (2001). "AKAP-Lbc anchors protein kinase A and nucleates Galpha 12-selective Rho-mediated stress fiber formation.". J. Biol. Chem. 276 (47): 44247–57. doi:10.1074/jbc.M106629200. PMID 11546812.
Kleer CG, van Golen KL, Zhang Y, et al. (2002). "Characterization of RhoC expression in benign and malignant breast disease: a potential new marker for small breast carcinomas with metastatic ability.". Am. J. Pathol. 160 (2): 579–84. doi:10.1016/S0002-9440(10)64877-8. PMC 1850656. PMID 11839578.
van Golen KL, Bao LW, Pan Q, et al. (2002). "Mitogen activated protein kinase pathway is involved in RhoC GTPase induced motility, invasion and angiogenesis in inflammatory breast cancer.". Clin. Exp. Metastasis 19 (4): 301–11. doi:10.1023/A:1015518114931. PMID 12090470.
Arthur WT, Ellerbroek SM, Der CJ, et al. (2003). "XPLN, a guanine nucleotide exchange factor for RhoA and RhoB, but not RhoC.". J. Biol. Chem. 277 (45): 42964–72. doi:10.1074/jbc.M207401200. PMID 12221096.
Shao F, Dixon JE (2003). "YopT is a cysteine protease cleaving Rho family GTPases.". Adv. Exp. Med. Biol. 529: 79–84. doi:10.1007/0-306-48416-1_14. PMID 12756732.

PDB gallery

1a2b: HUMAN RHOA COMPLEXED WITH GTP ANALOGUE

1cc0: CRYSTAL STRUCTURE OF THE RHOA.GDP-RHOGDI COMPLEX

1cxz: CRYSTAL STRUCTURE OF HUMAN RHOA COMPLEXED WITH THE EFFECTOR DOMAIN OF THE PROTEIN KINASE PKN/PRK1

1dpf: CRYSTAL STRUCTURE OF A MG-FREE FORM OF RHOA COMPLEXED WITH GDP

1ftn: CRYSTAL STRUCTURE OF THE HUMAN RHOA/GDP COMPLEX

1kmq: Crystal Structure of a Constitutively Activated RhoA Mutant (Q63L)

1lb1: Crystal Structure of the Dbl and Pleckstrin homology domains of Dbs in complex with RhoA

1ow3: Crystal Structure of RhoA.GDP.MgF3-in Complex with RhoGAP

1s1c: Crystal structure of the complex between the human RhoA and Rho-binding domain of human ROCKI

1tx4: RHO/RHOGAP/GDP(DOT)ALF4 COMPLEX

1x86: Crystal Structure of the DH/PH domains of Leukemia-associated RhoGEF in complex with RhoA

1xcg: Crystal Structure of Human RhoA in complex with DH/PH fragment of PDZRHOGEF

1z2c: Crystal structure of mDIA1 GBD-FH3 in complex with RhoC-GMPPNP

2gcn: Crystal structure of the human RhoC-GDP complex

2gco: Crystal structure of the human RhoC-GppNHp complex

2gcp: Crystal structure of the human RhoC-GSP complex

External links

UCSD-Nature Molecule Pages Published online: 16 Sep 2008 | doi:10.1038/mp.a002065.01
"RhoC : Abstract : UCSD-Nature Molecule Pages".

Hydrolases: acid anhydride hydrolases (EC 3.6)

3.6.1

3.6.2

3.6.3-4: ATPase

3.6.3

Cu++ (3.6.3.4)	Menkes/ATP7A Wilson/ATP7B

Ca+ (3.6.3.8)	SERCA ATP2A1 ATP2A2 ATP2A3 Plasma membrane ATP2B1 ATP2B2 ATP2B3 ATP2B4 SPCA ATP2C1 ATP2C2

Na+/K+ (3.6.3.9)	ATP1A1 ATP1A2 ATP1A3 ATP1A4 ATP1B1 ATP1B2 ATP1B3 ATP1B4

H+/K+ (3.6.3.10)	ATP4A

Other P-type ATPase	ATP8B1 ATP10A ATP11B ATP12A ATP13A2 ATP13A3

3.6.4

3.6.5: GTPase

3.6.5.1: Heterotrimeric G protein	G_αs G_αi GNAI1 GNAI2 GNAI3 G_αq/11 GNAQ GNA11 G_α12/13 GNA12 GNA13 Transducin GNAT1 GNAT2

3.6.5.2: Small GTPase > Ras superfamily	Rho family of GTPases: Cdc42 CDC42 TC10 TCL RhoUV RhoU RhoV Rac Rac1 2 3 RhoG RhoBTB 1 2 RhoH Rho A B C Rnd 1 2 3 RhoDF RhoF RhoD other: Ras HRAS KRAS NRAS Rab RAB23 RAB27 Arf ARF6 SAR1B ARL13B ARL6 Ran Rheb Rap RGK

3.6.5.3: Protein-synthesizing GTPase	Prokaryotic IF-2 EF-Tu EF-G Eukaryotic

3.6.5.5-6: Polymerization motors	Dynamin Tubulin

B
enzm
1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
2.1
- 2
- 3
- 4
- 5
- 6
- 7
  - 2.7.10
  - 11-12
- 8
3.1
- - 3.1.3.48
- 2
- 3
- 4
  - 3.4.21
  - 22
  - 23
  - 24
- 5
- 6
- 7
4.1
- 2
- 3
- 4
- 5
- 6
5.1
- 2
- 3
- 4
- 99
6.1-3
- 4
- 5-6

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RhoC

Mechanism and function

References

Further reading

External links