Biology:RALBP1
From HandWiki
Short description: Protein-coding gene in the species Homo sapiens
Generic protein structure example |
RalA-binding protein 1 is a protein that in humans is encoded by the RALBP1 gene.[1][2]
Interactions
RALBP1 has been shown to interact with:
References
- ↑ 1.0 1.1 1.2 "Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with CDC42/Rac GTPase-activating protein activity". J Biol Chem 270 (38): 22473–7. Oct 1995. doi:10.1074/jbc.270.38.22473. PMID 7673236.
- ↑ "Entrez Gene: RALBP1 ralA binding protein 1". https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=10928.
- ↑ "RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to phosphorylate epsin during the switch off of endocytosis in mitosis". J. Biol. Chem. 278 (33): 30597–604. Aug 2003. doi:10.1074/jbc.M302191200. PMID 12775724.
- ↑ "HSF-1 interacts with Ral-binding protein 1 in a stress-responsive, multiprotein complex with HSP90 in vivo". J. Biol. Chem. 278 (19): 17299–306. May 2003. doi:10.1074/jbc.M300788200. PMID 12621024.
- ↑ 5.0 5.1 "Ral GTPases regulate exocyst assembly through dual subunit interactions". J. Biol. Chem. 278 (51): 51743–8. Dec 2003. doi:10.1074/jbc.M308702200. PMID 14525976.
- ↑ "Identification and characterization of Ral-binding protein 1, a potential downstream target of Ral GTPases". Mol. Cell. Biol. 15 (8): 4578–84. Aug 1995. doi:10.1128/mcb.15.8.4578. PMID 7623849.
- ↑ 7.0 7.1 "Identification and characterization of a novel protein interacting with Ral-binding protein 1, a putative effector protein of Ral". J. Biol. Chem. 273 (2): 814–21. Jan 1998. doi:10.1074/jbc.273.2.814. PMID 9422736.
- ↑ "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. Oct 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R.
Further reading
- "RLIP76, a novel transporter catalyzing ATP-dependent efflux of xenobiotics". Drug Metab. Dispos. 30 (12): 1300–10. 2003. doi:10.1124/dmd.30.12.1300. PMID 12433796.
- "An Eps homology (EH) domain protein that binds to the Ral-GTPase target, RalBP1". J. Biol. Chem. 272 (50): 31230–4. 1998. doi:10.1074/jbc.272.50.31230. PMID 9395447.
- "Identification and characterization of a novel protein interacting with Ral-binding protein 1, a putative effector protein of Ral". J. Biol. Chem. 273 (2): 814–21. 1998. doi:10.1074/jbc.273.2.814. PMID 9422736.
- "Identification and characterization in Xenopus of XsmgGDS, a RalB binding protein". Biochem. Biophys. Res. Commun. 250 (2): 359–63. 1998. doi:10.1006/bbrc.1998.9336. PMID 9753634.
- "Involvement of Ras and Ral in Chemotactic Migration of Skeletal Myoblasts". Mol. Cell. Biol. 20 (13): 4658–65. 2000. doi:10.1128/MCB.20.13.4658-4665.2000. PMID 10848592.
- "RLIP76, an effector of the GTPase Ral, interacts with the AP2 complex: involvement of the Ral pathway in receptor endocytosis". J. Cell Sci. 113 (16): 2837–44. 2000. doi:10.1242/jcs.113.16.2837. PMID 10910768. https://hal.inrae.fr/hal-02696179/file/2000-Jullien-Flores_J%20cell%20Sci_1.pdf.
- "Novel function of human RLIP76: ATP-dependent transport of glutathione conjugates and doxorubicin". Biochemistry 39 (31): 9327–34. 2000. doi:10.1021/bi992964c. PMID 10924126.
- "RLIP76 is the major ATP-dependent transporter of glutathione-conjugates and doxorubicin in human erythrocytes". Arch. Biochem. Biophys. 391 (2): 171–9. 2001. doi:10.1006/abbi.2001.2395. PMID 11437348.
- "Purification and functional reconstitution of intact ral-binding Gtpase activating protein, RLIP76, in artificial liposomes". Acta Biochim. Pol. 48 (2): 551–62. 2002. doi:10.18388/abp.2001_3938. PMID 11732624.
- "Regulation of endocytosis of activin type II receptors by a novel PDZ protein through Ral/Ral-binding protein 1-dependent pathway". J. Biol. Chem. 277 (21): 19008–18. 2002. doi:10.1074/jbc.M112472200. PMID 11882656.
- "Role of RLIP76 in lung cancer doxorubicin resistance: I. The ATPase activity of RLIP76 correlates with doxorubicin and 4-hydroxynonenal resistance in lung cancer cells". Int. J. Oncol. 22 (2): 365–75. 2003. doi:10.3892/ijo.22.2.365. PMID 12527936.
- "Role of RLIP76 in lung cancer doxorubicin resistance: II. Doxorubicin transport in lung cancer by RLIP76". Int. J. Oncol. 22 (4): 713–20. 2003. doi:10.3892/ijo.22.4.713. PMID 12632060.
- "Role of RLIP76 in lung cancer doxorubicin resistance: III. Anti-RLIP76 antibodies trigger apoptosis in lung cancer cells and synergistically increase doxorubicin cytotoxicity". Int. J. Oncol. 22 (4): 721–32. 2003. doi:10.3892/ijo.22.4.721. PMID 12632061.
- "RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to phosphorylate epsin during the switch off of endocytosis in mitosis". J. Biol. Chem. 278 (33): 30597–604. 2003. doi:10.1074/jbc.M302191200. PMID 12775724.
- "Ral GTPases regulate exocyst assembly through dual subunit interactions". J. Biol. Chem. 278 (51): 51743–8. 2004. doi:10.1074/jbc.M308702200. PMID 14525976.
- "Staphylococcus aureus protein A induces airway epithelial inflammatory responses by activating TNFR1". Nat. Med. 10 (8): 842–8. 2004. doi:10.1038/nm1079. PMID 15247912.
- "AIP1/DAB2IP, a novel member of the Ras-GAP family, transduces TRAF2-induced ASK1-JNK activation". J. Biol. Chem. 279 (43): 44955–65. 2004. doi:10.1074/jbc.M407617200. PMID 15310755.
