BIN1

BIN1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1MUZ, 1MV0, 1MV3, 2FIC, 2RMY, 2RND, 5I22
Identifiers
Aliases	BIN1 , AMPH2, AMPHL, SH3P9, bridging integrator 1, CNM2
External IDs	OMIM: 601248 MGI: 108092 HomoloGene: 113707 GeneCards: BIN1
Gene location (Human) Chr. Chromosome 2 (human) [1] Band 2q14.3 Start 127,048,027 bp [1] End 127,107,288 bp [1]
Gene location (Mouse) Chr. Chromosome 18 (mouse) [2] Band 18 B1|18 18.01 cM Start 32,510,283 bp [2] End 32,568,790 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in gastrocnemius muscle tibialis anterior muscle quadriceps femoris muscle vastus lateralis muscle triceps brachii muscle thoracic diaphragm deltoid muscle biceps brachii middle frontal gyrus corpus callosum Top expressed in triceps brachii muscle temporal muscle extensor digitorum longus muscle sternocleidomastoid muscle plantaris muscle skeletal muscle tissue digastric muscle ankle tibialis anterior muscle soleus muscle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding RNA polymerase binding identical protein binding tau protein binding actin filament binding protease binding phospholipid binding clathrin binding chaperone binding Cellular component cytoplasm membrane I band T-tubule lipid tube node of Ranvier axon Z disc actin cytoskeleton axon initial segment nucleus nuclear envelope cytosol endosome cytoskeleton plasma membrane synaptic vesicle sarcolemma synapse Biological process regulation of endocytosis regulation of neuron differentiation cell differentiation endocytosis positive regulation of astrocyte differentiation multicellular organism development muscle cell differentiation positive regulation of apoptotic process lipid tube assembly cell population proliferation viral process nucleus localization nucleus organization membrane organization cytoskeleton organization endosome to lysosome transport positive regulation of actin filament polymerization T-tubule organization regulation of heart rate by cardiac conduction negative regulation of potassium ion transmembrane transport negative regulation of amyloid-beta formation negative regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process negative regulation of ventricular cardiac muscle cell action potential negative regulation of calcium ion transmembrane transport via high voltage-gated calcium channel Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 274 30948 Ensembl ENSG00000136717 ENSMUSG00000024381 UniProt O00499 O08539 RefSeq (mRNA) NM_004305 NM_139343 NM_139344 NM_139345 NM_139346 NM_139347 NM_139348 NM_139349 NM_139350 NM_139351 NM_001320632 NM_001320633 NM_001320634 NM_001320640 NM_001320641 NM_001320642 NM_001083334 NM_009668 NM_001360876 RefSeq (protein) NP_001307561 NP_001307562 NP_001307563 NP_001307569 NP_001307570 NP_001307571 NP_004296 NP_647593 NP_647594 NP_647595 NP_647596 NP_647597 NP_647598 NP_647599 NP_647600 NP_647601 NP_647601.1 NP_001307561.1 NP_001076803 NP_033798 NP_001347805 Location (UCSC) Chr 2: 127.05 – 127.11 Mb Chr 18: 32.51 – 32.57 Mb PubMed search [3] [4]
Wikidata
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Myc box-dependent-interacting protein 1, also known as Bridging Integrator-1 and Amphiphysin-2 is a protein that in humans is encoded by the BIN1 gene. ^{[5] [6] [7]}

This gene encodes several isoforms of a nucleocytoplasmic adaptor protein, one of which was initially identified as a MYC-interacting protein with features of a tumor suppressor.

Isoforms that are expressed in the central nervous system may be involved in synaptic vesicle endocytosis and may interact with dynanim, synaptojanin, endophilin, and clathrin. ^[8]

Isoforms that are expressed in muscle and ubiquitously expressed isoforms localize to the cytoplasm and nucleus and activate a caspase-independent apoptotic process. ^[8]

Studies in mouse suggest that this gene plays an important role in cardiac muscle development. Alternate splicing of the gene results in ten transcript variants encoding different isoforms. Aberrant splice variants expressed in tumor cell lines have also been described. ^[8]

Clinical significance

In humans, mutations in BIN1 have been associated with skeletal myopathies including centronuclear myopathy causing muscle weakness ^[7] and myotonic dystrophy causing progressive muscle wasting, myotonia, cataracts, and heart conduction defects. ^[9] An association has also been found between BIN1 mutations and Alzheimer's disease. ^[9] Knockdown of BIN1 produces a cardiomyopathy phenotype in zebrafish, ^[10] and in sheep BIN1 may be responsible for the loss of T-tubules seen in heart failure. ^[11]

Interactions

BIN1 has been shown to interact with Phospholipase D1, ^[12] SNX4 ^[13] and PLD2. ^[12]

References

1. GRCh38: Ensembl release 89: ENSG00000136717 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000024381 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Negorev D, Riethman H, Wechsler-Reya R, Sakamuro D, Prendergast GC, Simon D (January 1997). "The Bin1 gene localizes to human chromosome 2q14 by PCR analysis of somatic cell hybrids and fluorescence in situ hybridization". Genomics. 33 (2): 329–31. doi:10.1006/geno.1996.0205. PMID   8725406.
6. Sakamuro D, Elliott KJ, Wechsler-Reya R, Prendergast GC (October 1996). "BIN1 is a novel MYC-interacting protein with features of a tumour suppressor". Nat Genet. 14 (1): 69–77. doi:10.1038/ng0996-69. PMID   8782822. S2CID   21484402.
7. Nicot AS, Toussaint A, Tosch V, Kretz C, Wallgren-Pettersson C, Iwarsson E, Kingston H, Garnier JM, Biancalana V, Oldfors A, Mandel JL, Laporte J (August 2007). "Mutations in amphiphysin 2 (BIN1) disrupt interaction with dynamin 2 and cause autosomal recessive centronuclear myopathy". Nat Genet. 39 (9): 1134–9. doi:10.1038/ng2086. PMID   17676042. S2CID   16861439.
8. "Entrez Gene: BIN1 bridging integrator 1".
9. Prokic I, Cowling BS, Laporte J (May 2014). "Amphiphysin 2 (BIN1) in physiology and diseases". Journal of Molecular Medicine. 92 (5): 453–463. doi:10.1007/s00109-014-1138-1. ISSN   1432-1440. PMID   24590001. S2CID   14038898.
10. Hong T, Smyth JW, Chu KY, Vogan JM, Fong TS, Jensen BC, Fang K, Halushka MK, Russell SD (May 2012). "BIN1 is reduced and Cav1.2 trafficking is impaired in human failing cardiomyocytes". Heart Rhythm. 9 (5): 812–820. doi:10.1016/j.hrthm.2011.11.055. ISSN   1556-3871. PMC   3306544 . PMID   22138472.
11. Caldwell JL, Smith CE, Taylor RF, Kitmitto A, Eisner DA, Dibb KM, Trafford AW (2014-12-05). "Dependence of cardiac transverse tubules on the BAR domain protein amphiphysin II (BIN-1)". Circulation Research. 115 (12): 986–996. doi:10.1161/CIRCRESAHA.116.303448. ISSN   1524-4571. PMC   4274343 . PMID   25332206.
12. Lee C, Kim S R, Chung J K, Frohman M A, Kilimann M W, Rhee S G (June 2000). "Inhibition of phospholipase D by amphiphysins". J. Biol. Chem. 275 (25): 18751–8. doi: 10.1074/jbc.M001695200 . ISSN   0021-9258. PMID   10764771.
13. Leprince C, Le Scolan Erwan, Meunier Brigitte, Fraisier Vincent, Brandon Nathalie, De Gunzburg Jean, Camonis Jacques (May 2003). "Sorting nexin 4 and amphiphysin 2, a new partnership between endocytosis and intracellular trafficking". J. Cell Sci. 116 (Pt 10): 1937–48. doi: 10.1242/jcs.00403 . ISSN   0021-9533. PMID   12668730.

Further reading

• Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID   8619474.
• Yu W, Andersson B, Worley KC, et al. (1997). "Large-Scale Concatenation cDNA Sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC   139146 . PMID   9110174.
• Leprince C, Romero F, Cussac D, et al. (1997). "A new member of the amphiphysin family connecting endocytosis and signal transduction pathways". J. Biol. Chem. 272 (24): 15101–5. doi: 10.1074/jbc.272.24.15101 . PMID   9182529.
• Butler MH, David C, Ochoa GC, et al. (1997). "Amphiphysin II (SH3P9; BIN1), a Member of the Amphiphysin/Rvs Family, Is Concentrated in the Cortical Cytomatrix of Axon Initial Segments and Nodes of Ranvier in Brain and around T Tubules in Skeletal Muscle". J. Cell Biol. 137 (6): 1355–67. doi:10.1083/jcb.137.6.1355. PMC   2132527 . PMID   9182667.
• Ramjaun AR, Micheva KD, Bouchelet I, McPherson PS (1997). "Identification and characterization of a nerve terminal-enriched amphiphysin isoform". J. Biol. Chem. 272 (26): 16700–6. doi: 10.1074/jbc.272.26.16700 . PMID   9195986.
• Tsutsui K, Maeda Y, Tsutsui K, et al. (1997). "cDNA cloning of a novel amphiphysin isoform and tissue-specific expression of its multiple splice variants". Biochem. Biophys. Res. Commun. 236 (1): 178–83. doi:10.1006/bbrc.1997.6927. PMID   9223448.
• McMahon HT, Wigge P, Smith C (1997). "Clathrin interacts specifically with amphiphysin and is displaced by dynamin". FEBS Lett. 413 (2): 319–22. doi: 10.1016/S0014-5793(97)00928-9 . PMID   9280305. S2CID   42520828.
• Micheva KD, Ramjaun AR, Kay BK, McPherson PS (1997). "SH3 domain-dependent interactions of endophilin with amphiphysin". FEBS Lett. 414 (2): 308–12. doi: 10.1016/S0014-5793(97)01016-8 . PMID   9315708. S2CID   21328416.
• Micheva KD, Kay BK, McPherson PS (1997). "Synaptojanin forms two separate complexes in the nerve terminal. Interactions with endophilin and amphiphysin". J. Biol. Chem. 272 (43): 27239–45. doi: 10.1074/jbc.272.43.27239 . PMID   9341169.
• Wigge P, Köhler K, Vallis Y, et al. (1997). "Amphiphysin Heterodimers: Potential Role in Clathrin-mediated Endocytosis". Mol. Biol. Cell. 8 (10): 2003–15. doi:10.1091/mbc.8.10.2003. PMC   25662 . PMID   9348539.
• Kadlec L, Pendergast AM (1997). "The amphiphysin-like protein 1 (ALP1) interacts functionally with the cABL tyrosine kinase and may play a role in cytoskeletal regulation". Proc. Natl. Acad. Sci. U.S.A. 94 (23): 12390–5. Bibcode:1997PNAS...9412390K. doi: 10.1073/pnas.94.23.12390 . PMC   24959 . PMID   9356459.
• Wechsler-Reya R, Sakamuro D, Zhang J, et al. (1998). "Structural analysis of the human BIN1 gene. Evidence for tissue-specific transcriptional regulation and alternate RNA splicing". J. Biol. Chem. 272 (50): 31453–8. doi: 10.1074/jbc.272.50.31453 . PMID   9395479.
• Wechsler-Reya RJ, Elliott KJ, Prendergast GC (1998). "A Role for the Putative Tumor Suppressor Bin1 in Muscle Cell Differentiation". Mol. Cell. Biol. 18 (1): 566–75. doi:10.1128/MCB.18.1.566. PMC   121524 . PMID   9418903.
• Ramjaun AR, McPherson PS (1998). "Multiple amphiphysin II splice variants display differential clathrin binding: identification of two distinct clathrin-binding sites". J. Neurochem. 70 (6): 2369–76. doi: 10.1046/j.1471-4159.1998.70062369.x . PMID   9603201. S2CID   21910795.
• Mao NC, Steingrimsson E, DuHadaway J, et al. (1999). "The murine Bin1 gene functions early in myogenesis and defines a new region of synteny between mouse chromosome 18 and human chromosome 2". Genomics. 56 (1): 51–8. doi:10.1006/geno.1998.5709. PMID   10036185.
• Wixler V, Laplantine E, Geerts D, et al. (1999). "Identification of novel interaction partners for the conserved membrane proximal region of alpha-integrin cytoplasmic domains". FEBS Lett. 445 (2–3): 351–5. doi: 10.1016/S0014-5793(99)00151-9 . PMID   10094488. S2CID   9218762.
• Ramjaun AR, Philie J, de Heuvel E, McPherson PS (1999). "The N terminus of amphiphysin II mediates dimerization and plasma membrane targeting". J. Biol. Chem. 274 (28): 19785–91. doi: 10.1074/jbc.274.28.19785 . PMID   10391921.
• Traub LM, Downs MA, Westrich JL, Fremont DH (1999). "Crystal structure of the α appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly". Proc. Natl. Acad. Sci. U.S.A. 96 (16): 8907–12. Bibcode:1999PNAS...96.8907T. doi: 10.1073/pnas.96.16.8907 . PMC   17706 . PMID   10430869.
• "Genetic study of Lewy body dementia supports ties to Alzheimer's and Parkinson's diseases". National Institutes of Health (NIH). 2021-02-16. Retrieved 2023-08-07.

External links

• Human BIN1 genome location and BIN1 gene details page in the UCSC Genome Browser .