| 词条 | RhoBTB |
| 释义 |
| Name = Rho-related BTB domain containing 1 | caption = | image = | width = | HGNCid = 18738 | Symbol = RHOBTB1 | AltSymbols = | EntrezGene = 9886 | OMIM = 607351 | RefSeq = NM_014836 | UniProt = O94844 | PDB = | ECnumber = | Chromosome = 10 | Arm = q | Band = 22.1 | LocusSupplementaryData = }}{{infobox protein | Name = Rho-related BTB domain containing 2 | caption = | image = | width = | HGNCid = 18756 | Symbol = RHOBTB2 | AltSymbols = | EntrezGene = 23221 | OMIM = 607352 | RefSeq = NM_001160036 | UniProt = Q9BYZ6 | PDB = | ECnumber = | Chromosome = 8 | Arm = p | Band = 21.2 | LocusSupplementaryData = }}{{infobox protein | Name = Rho-related BTB domain containing 3 | caption = | image = | width = | HGNCid = 18757 | Symbol = RHOBTB3 | AltSymbols = | EntrezGene = 22836 | OMIM = 607353 | RefSeq = NM_014899 | UniProt = O94955 | PDB = | ECnumber = | Chromosome = 5 | Arm = q | Band = 15 | LocusSupplementaryData = }} The RhoBTB family is a subgroup of the Rho family of small GTPases. They are a highly divergent class and are all characterized by an N-terminal Rho-related domain followed by at least one C-terminal BTB domain. DiscoveryThe RhoBTB family of molecules was unknowingly discovered in 1993 by analyzing the Dictyostelium genome looking for members of the Ras superfamily of GTPases. The authors began by doing Southern blots looking for cDNAs that cross-hybridize with a very conservative probe from hRas.[1] They identified 19 new genes that belonged to the Ras superfamily and sequenced approximately 600 nucleotides from the start of the transcript.[1] If they were looking for a normal Ras-like GTPase, this would have been sufficient. One of their clones, they called RacA, was more divergent than most of the others and the transcript didn’t terminate in a stop codon like the rest.[1] The authors, however, didn’t comment on this and RhoBTB went undiscovered for another eight years. A very careful analysis by Francisco Rivero and coworkers ensued to find all of the Rho GTPases in Dictyostelium. During their endeavor, they found that the open reading frame of RacA was actually 400 amino acids longer than what Bush had published 8 years earlier.[2] Instead of a 168 amino acid protein, RacA encoded a 598 residue protein with a Rho GTPase domain at the N-terminus and two BTB domains toward the C-terminus. BTB (Broad-Complex, Tramtrack and Bric-a-Brac) domains are known to involve hetero and homo associations with other BTB domain-containing proteins.[3][4] Because this novel RhoBTB protein was in Dictostelium, the authors were curious if any homologous proteins exist in humans. They found three and called them RhoBTB1, RhoBTB2, and RhoBTB3.[2] Localization and expressionRhoBTB1 and RhoBTB2 are much more homologous than RhoBTB3.[2] Further analysis revealed that the intron-exon structure of RhoBTB1 and 2 are also quite similar and have only one common intron with RhoBTB3.[5] RhoBTB1 and 2 were not detected during mouse development, but RhoBTB3 was detected strongly between embryonic days 11.5 through 17.5.[5] Additionally, RhoBTB1 and 2 are localized to vesicular structures,[6] while RhoBTB3 is localized to the trans-Golgi network.[7] References1. ^1 2 {{cite journal |vauthors=Bush J, Franek K, Cardelli J | title = Cloning and characterization of seven novel Dictyostelium discoideum rac-related genes belonging to the rho family of GTPases | journal = Gene | volume = 136 | issue = 1–2 | pages = 61–8 |date=December 1993 | pmid = 8294042 | doi = 10.1016/0378-1119(93)90448-C| url = }} 2. ^1 2 {{cite journal |vauthors=Rivero F, Dislich H, Glöckner G, Noegel AA | title = The Dictyostelium discoideum family of Rho-related proteins | journal = Nucleic Acids Res. | volume = 29 | issue = 5 | pages = 1068–79 |date=March 2001 | pmid = 11222756 | pmc = 29714 | doi = 10.1093/nar/29.5.1068| url = }} 3. ^{{cite journal |vauthors=Zollman S, Godt D, Privé GG, Couderc JL, Laski FA | title = The BTB domain, found primarily in zinc finger proteins, defines an evolutionarily conserved family that includes several developmentally regulated genes in Drosophila | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 91 | issue = 22 | pages = 10717–21 |date=October 1994 | pmid = 7938017 | pmc = 45093 | doi = 10.1073/pnas.91.22.10717| url = }} 4. ^{{cite journal |vauthors=Ahmad KF, Engel CK, Privé GG | title = Crystal structure of the BTB domain from PLZF | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 95 | issue = 21 | pages = 12123–8 |date=October 1998 | pmid = 9770450 | pmc = 22795 | doi = 10.1073/pnas.95.21.12123| url = }} 5. ^1 {{cite journal |vauthors=Ramos S, Khademi F, Somesh BP, Rivero F | title = Genomic organization and expression profile of the small GTPases of the RhoBTB family in human and mouse | journal = Gene | volume = 298 | issue = 2 | pages = 147–57 |date=October 2002 | pmid = 12426103 | doi = 10.1016/S0378-1119(02)00980-0| url = }} 6. ^{{cite journal |vauthors=Aspenström P, Fransson A, Saras J | title = Rho GTPases have diverse effects on the organization of the actin filament system | journal = Biochem. J. | volume = 377 | issue = Pt 2 | pages = 327–37 |date=January 2004 | pmid = 14521508 | pmc = 1223866 | doi = 10.1042/BJ20031041 | url = }} 7. ^{{cite journal |vauthors=Espinosa EJ, Calero M, Sridevi K, Pfeffer SR | title = RhoBTB3: A Rho GTPase-family ATPase required for endosome to Golgi transport | journal = Cell | volume = 137 | issue = 5 | pages = 938–48 |date=May 2009 | pmid = 19490898 | pmc = 2801561 | doi = 10.1016/j.cell.2009.03.043 | url = }} |
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