Biology:APBB1

Short description: Protein-coding gene in the species Homo sapiens

Generic protein structure example

Amyloid beta A4 precursor protein-binding family B member 1 is a protein that in humans is encoded by the APBB1 gene.

Function

The protein encoded by this gene is a member of the Fe65 protein family. It is an adaptor protein localized in the nucleus. It interacts with the Alzheimer's disease amyloid precursor protein (APP), transcription factor CP2/LSF/LBP1 and the low-density lipoprotein receptor-related protein. APP functions as a cytosolic anchoring site that can prevent the gene product's nuclear translocation. This encoded protein could play an important role in the pathogenesis of Alzheimer's disease. It is thought to regulate transcription. Also it is observed to block cell cycle progression by downregulating thymidylate synthase expression. Multiple alternatively spliced transcript variants have been described for this gene but some of their full length sequence is not known.

Interactions

APBB1 has been shown to interact with APLP2, TFCP2, LRP1 and Amyloid precursor protein.

External links

• Human APBB1 genome location and APBB1 gene details page in the UCSC Genome Browser.

Further reading

• "Fe65 and the protein network centered around the cytosolic domain of the Alzheimer's beta-amyloid precursor protein". FEBS Lett. 434 (1–2): 1–7. 1998. doi:10.1016/S0014-5793(98)00941-7. PMID 9738440. 
• "Proposed pathogenetic cascade of inclusion-body myositis: importance of amyloid-beta, misfolded proteins, predisposing genes, and aging". Current Opinion in Rheumatology 15 (6): 737–44. 2004. doi:10.1097/00002281-200311000-00009. PMID 14569203. 
• "The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein". Mol. Cell. Biol. 16 (11): 6229–41. 1996. doi:10.1128/mcb.16.11.6229. PMID 8887653. 
• "Interaction of the phosphotyrosine interaction/phosphotyrosine binding-related domains of Fe65 with wild-type and mutant Alzheimer's beta-amyloid precursor proteins". J. Biol. Chem. 272 (10): 6399–405. 1997. doi:10.1074/jbc.272.10.6399. PMID 9045663. 
• "The WW domain of neural protein FE65 interacts with proline-rich motifs in Mena, the mammalian homolog of Drosophila enabled". J. Biol. Chem. 272 (52): 32869–77. 1998. doi:10.1074/jbc.272.52.32869. PMID 9407065. 
• "Fe65L2: a new member of the Fe65 protein family interacting with the intracellular domain of the Alzheimer's beta-amyloid precursor protein". Biochem. J. 330 (Pt 1): 513–9. 1998. doi:10.1042/bj3300513. PMID 9461550. 
• "Mapping of the human and murine X11-like genes (APBA2 and apba2), the murine Fe65 gene (Apbb1), and the human Fe65-like gene (APBB2): genes encoding phosphotyrosine-binding domain proteins that interact with the Alzheimer's disease amyloid precursor protein". Mamm. Genome 9 (6): 473–5. 1998. doi:10.1007/s003359900800. PMID 9585438. 
• "The Fe65 adaptor protein interacts through its PID1 domain with the transcription factor CP2/LSF/LBP1". J. Biol. Chem. 273 (32): 20128–33. 1998. doi:10.1074/jbc.273.32.20128. PMID 9685356. 
• "The human FE65 gene: genomic structure and an intronic biallelic polymorphism associated with sporadic dementia of the Alzheimer type". Hum. Genet. 103 (3): 295–303. 1998. doi:10.1007/s004390050820. PMID 9799084. 
• "Interaction of cytosolic adaptor proteins with neuronal apolipoprotein E receptors and the amyloid precursor protein". J. Biol. Chem. 273 (50): 33556–60. 1999. doi:10.1074/jbc.273.50.33556. PMID 9837937. 
• "Regulation of beta-amyloid secretion by FE65, an amyloid protein precursor-binding protein". J. Biol. Chem. 274 (12): 7952–7. 1999. doi:10.1074/jbc.274.12.7952. PMID 10075692. 
• "Alternatively spliced isoforms of FE65 serve as neuron-specific and non-neuronal markers". J. Neurosci. Res. 58 (5): 632–40. 2000. doi:10.1002/(SICI)1097-4547(19991201)58:5<632::AID-JNR4>3.0.CO;2-P. PMID 10561691. 
• "cAMP-dependent protein kinase phosphorylation of EVL, a Mena/VASP relative, regulates its interaction with actin and SH3 domains". J. Biol. Chem. 275 (46): 36143–51. 2000. doi:10.1074/jbc.M006274200. PMID 10945997. 
• "The beta-amyloid precursor protein functions as a cytosolic anchoring site that prevents Fe65 nuclear translocation". J. Biol. Chem. 276 (9): 6545–50. 2001. doi:10.1074/jbc.M007340200. PMID 11085987. 
• "Fe65 and X11beta co-localize with and compete for binding to the amyloid precursor protein". NeuroReport 11 (16): 3607–10. 2001. doi:10.1097/00001756-200011090-00041. PMID 11095528. 
• "The neuronal adaptor protein X11alpha interacts with the copper chaperone for SOD1 and regulates SOD1 activity". J. Biol. Chem. 276 (12): 9303–7. 2001. doi:10.1074/jbc.M010023200. PMID 11115513. 
• "The beta-amyloid precursor protein APP is tyrosine-phosphorylated in cells expressing a constitutively active form of the Abl protoncogene". J. Biol. Chem. 276 (23): 19787–92. 2001. doi:10.1074/jbc.M100792200. PMID 11279131.