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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]].<ref name="pmid8725406">{{cite journal | vauthors = Negorev D, Riethman H, Wechsler-Reya R, Sakamuro D, Prendergast GC, Simon D | title = The Bin1 gene localizes to human chromosome 2q14 by PCR analysis of somatic cell hybrids and fluorescence in situ hybridization | journal = Genomics | volume = 33 | issue = 2 | pages = 329–31 |date=January 1997 | pmid = 8725406 | pmc = | doi = 10.1006/geno.1996.0205 }}</ref><ref name="pmid8782822">{{cite journal | vauthors = Sakamuro D, Elliott KJ, Wechsler-Reya R, Prendergast GC | title = BIN1 is a novel MYC-interacting protein with features of a tumour suppressor | journal = Nat Genet | volume = 14 | issue = 1 | pages = 69–77 |date=October 1996 | pmid = 8782822 | pmc = | doi = 10.1038/ng0996-69 }}</ref><ref name="pmid17676042">{{cite journal | vauthors = 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 | title = Mutations in amphiphysin 2 (BIN1) disrupt interaction with dynamin 2 and cause autosomal recessive centronuclear myopathy | journal = Nat Genet | volume = 39 | issue = 9 | pages = 1134–9 |date=August 2007 | pmid = 17676042 | pmc = | doi = 10.1038/ng2086 }}</ref> | ||
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{{PBB_Summary | {{PBB_Summary | ||
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| summary_text = 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. Isoforms that are expressed in muscle and ubiquitously expressed isoforms localize to the cytoplasm and nucleus and activate a caspase-independent apoptotic process. 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.<ref name="entrez">{{cite web | title = Entrez Gene: BIN1 bridging integrator 1| url = | | summary_text = This gene encodes several isoforms of a nucleocytoplasmic [[Signal transducing adaptor protein|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.<ref name="entrez"/> | |||
Isoforms that are expressed in muscle and ubiquitously expressed isoforms localize to the cytoplasm and nucleus and activate a caspase-independent apoptotic process.<ref name="entrez"/> | |||
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.<ref name="entrez">{{cite web | title = Entrez Gene: BIN1 bridging integrator 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=274| accessdate = }}</ref> | |||
}} | }} | ||
==Clinical significance== | |||
In humans, mutations in BIN1 have been associated with skeletal myopathies including centronuclear [[myopathy]] causing muscle weakness<ref name="pmid17676042"/> and myotonic dystrophy causing progressive muscle wasting, myotonia, cataracts, and heart conduction defects.<ref name=":0">{{Cite journal|last=Prokic|first=Ivana|last2=Cowling|first2=Belinda S.|last3=Laporte|first3=Jocelyn|date=May 2014|title=Amphiphysin 2 (BIN1) in physiology and diseases|journal=Journal of Molecular Medicine (Berlin, Germany)|volume=92|issue=5|pages=453–463|doi=10.1007/s00109-014-1138-1|issn=1432-1440|pmid=24590001}}</ref> An association has also been found between BIN1 mutations and Alzheimer's disease.<ref name=":0" /> Knockdown of BIN1 in produces a cardiomyopathy phenotype in zebrafish,<ref>{{Cite journal|last=Hong|first=Ting-Ting|last2=Smyth|first2=James W.|last3=Chu|first3=Kevin Y.|last4=Vogan|first4=Jacob M.|last5=Fong|first5=Tina S.|last6=Jensen|first6=Brian C.|last7=Fang|first7=Kun|last8=Halushka|first8=Marc K.|last9=Russell|first9=Stuart D.|date=May 2012|title=BIN1 is reduced and Cav1.2 trafficking is impaired in human failing cardiomyocytes|journal=Heart Rhythm|volume=9|issue=5|pages=812–820|doi=10.1016/j.hrthm.2011.11.055|issn=1556-3871|pmc=3306544|pmid=22138472}}</ref> and in sheep BIN1 may be responsible for the loss of T-tubules seen in heart failure.<ref>{{Cite journal|last=Caldwell|first=Jessica L.|last2=Smith|first2=Charlotte E. R.|last3=Taylor|first3=Rebecca F.|last4=Kitmitto|first4=Ashraf|last5=Eisner|first5=David A.|last6=Dibb|first6=Katharine M.|last7=Trafford|first7=Andrew W.|date=2014-12-05|title=Dependence of cardiac transverse tubules on the BAR domain protein amphiphysin II (BIN-1)|journal=Circulation Research|volume=115|issue=12|pages=986–996|doi=10.1161/CIRCRESAHA.116.303448|issn=1524-4571|pmc=4274343|pmid=25332206}}</ref> | |||
==Interactions== | |||
BIN1 has been shown to [[Protein-protein interaction|interact]] with [[Phospholipase D1]],<ref name=pmid10764771>{{cite journal |last=Lee |first=C |author2=Kim S R|author3=Chung J K|author4=Frohman M A|author5=Kilimann M W|author6=Rhee S G |date=June 2000 |title=Inhibition of phospholipase D by amphiphysins |journal=J. Biol. Chem. |volume=275 |issue=25 |pages=18751–8 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 10764771 |doi = 10.1074/jbc.M001695200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> [[SNX4]]<ref name=pmid12668730>{{cite journal |last=Leprince |first=Corinne |author2=Le Scolan Erwan |author3=Meunier Brigitte |author4=Fraisier Vincent |author5=Brandon Nathalie |author6=De Gunzburg Jean |author7=Camonis Jacques |date=May 2003 |title=Sorting nexin 4 and amphiphysin 2, a new partnership between endocytosis and intracellular trafficking |journal=J. Cell Sci. |volume=116 |issue=Pt 10 |pages=1937–48 |publisher= |location = England| issn = 0021-9533| pmid = 12668730 |doi = 10.1242/jcs.00403 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> and [[PLD2]].<ref name=pmid10764771/> | |||
==References== | ==References== | ||
{{reflist | {{reflist}} | ||
==Further reading== | ==Further reading== | ||
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| citations = | | citations = | ||
*{{cite journal | | *{{cite journal | vauthors=Andersson B, Wentland MA, Ricafrente JY |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107–13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Yu W, Andersson B, Worley KC |title=Large-Scale Concatenation cDNA Sequencing |journal=Genome Res. |volume=7 |issue= 4 |pages= 353–8 |year= 1997 |pmid= 9110174 |doi= 10.1101/gr.7.4.353| pmc=139146 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Leprince C, Romero F, Cussac D |title=A new member of the amphiphysin family connecting endocytosis and signal transduction pathways |journal=J. Biol. Chem. |volume=272 |issue= 24 |pages= 15101–5 |year= 1997 |pmid= 9182529 |doi=10.1074/jbc.272.24.15101 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Butler MH, David C, Ochoa GC |title=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 |journal=J. Cell Biol. |volume=137 |issue= 6 |pages= 1355–67 |year= 1997 |pmid= 9182667 |doi=10.1083/jcb.137.6.1355 | pmc=2132527 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Ramjaun AR, Micheva KD, Bouchelet I, McPherson PS |title=Identification and characterization of a nerve terminal-enriched amphiphysin isoform |journal=J. Biol. Chem. |volume=272 |issue= 26 |pages= 16700–6 |year= 1997 |pmid= 9195986 |doi=10.1074/jbc.272.26.16700 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Tsutsui K, Maeda Y, Tsutsui K |title=cDNA cloning of a novel amphiphysin isoform and tissue-specific expression of its multiple splice variants |journal=Biochem. Biophys. Res. Commun. |volume=236 |issue= 1 |pages= 178–83 |year= 1997 |pmid= 9223448 |doi= 10.1006/bbrc.1997.6927 |display-authors=etal}} | ||
*{{cite journal | vauthors=McMahon HT, Wigge P, Smith C |title=Clathrin interacts specifically with amphiphysin and is displaced by dynamin |journal=FEBS Lett. |volume=413 |issue= 2 |pages= 319–22 |year= 1997 |pmid= 9280305 |doi=10.1016/S0014-5793(97)00928-9 }} | |||
*{{cite journal | | *{{cite journal | vauthors=Micheva KD, Ramjaun AR, Kay BK, McPherson PS |title=SH3 domain-dependent interactions of endophilin with amphiphysin |journal=FEBS Lett. |volume=414 |issue= 2 |pages= 308–12 |year= 1997 |pmid= 9315708 |doi=10.1016/S0014-5793(97)01016-8 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Micheva KD, Kay BK, McPherson PS |title=Synaptojanin forms two separate complexes in the nerve terminal. Interactions with endophilin and amphiphysin |journal=J. Biol. Chem. |volume=272 |issue= 43 |pages= 27239–45 |year= 1997 |pmid= 9341169 |doi=10.1074/jbc.272.43.27239 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Wigge P, Köhler K, Vallis Y |title=Amphiphysin Heterodimers: Potential Role in Clathrin-mediated Endocytosis |journal=Mol. Biol. Cell |volume=8 |issue= 10 |pages= 2003–15 |year= 1997 |pmid= 9348539 |doi= 10.1091/mbc.8.10.2003| pmc=25662 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Kadlec L, Pendergast AM |title=The amphiphysin-like protein 1 (ALP1) interacts functionally with the cABL tyrosine kinase and may play a role in cytoskeletal regulation |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 23 |pages= 12390–5 |year= 1997 |pmid= 9356459 |doi=10.1073/pnas.94.23.12390 | pmc=24959 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Wechsler-Reya R, Sakamuro D, Zhang J |title=Structural analysis of the human BIN1 gene. Evidence for tissue-specific transcriptional regulation and alternate RNA splicing |journal=J. Biol. Chem. |volume=272 |issue= 50 |pages= 31453–8 |year= 1998 |pmid= 9395479 |doi=10.1074/jbc.272.50.31453 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Wechsler-Reya RJ, Elliott KJ, Prendergast GC |title=A Role for the Putative Tumor Suppressor Bin1 in Muscle Cell Differentiation |journal=Mol. Cell. Biol. |volume=18 |issue= 1 |pages= 566–75 |year= 1998 |pmid= 9418903 |doi= | pmc=121524 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Ramjaun AR, McPherson PS |title=Multiple amphiphysin II splice variants display differential clathrin binding: identification of two distinct clathrin-binding sites |journal=J. Neurochem. |volume=70 |issue= 6 |pages= 2369–76 |year= 1998 |pmid= 9603201 |doi=10.1046/j.1471-4159.1998.70062369.x }} | ||
*{{cite journal | | *{{cite journal | vauthors=Mao NC, Steingrimsson E, DuHadaway J |title=The murine Bin1 gene functions early in myogenesis and defines a new region of synteny between mouse chromosome 18 and human chromosome 2 |journal=Genomics |volume=56 |issue= 1 |pages= 51–8 |year= 1999 |pmid= 10036185 |doi= 10.1006/geno.1998.5709 |display-authors=etal}} | ||
*{{cite journal | vauthors=Wixler V, Laplantine E, Geerts D |title=Identification of novel interaction partners for the conserved membrane proximal region of alpha-integrin cytoplasmic domains |journal=FEBS Lett. |volume=445 |issue= 2–3 |pages= 351–5 |year= 1999 |pmid= 10094488 |doi=10.1016/S0014-5793(99)00151-9 |display-authors=etal}} | |||
*{{cite journal | | *{{cite journal | vauthors=Ramjaun AR, Philie J, de Heuvel E, McPherson PS |title=The N terminus of amphiphysin II mediates dimerization and plasma membrane targeting |journal=J. Biol. Chem. |volume=274 |issue= 28 |pages= 19785–91 |year= 1999 |pmid= 10391921 |doi=10.1074/jbc.274.28.19785 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Traub LM, Downs MA, Westrich JL, Fremont DH |title=Crystal structure of the α appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 16 |pages= 8907–12 |year= 1999 |pmid= 10430869 |doi=10.1073/pnas.96.16.8907 | pmc=17706 }} | ||
}} | }} | ||
{{refend}} | {{refend}} | ||
{{ | ==External links== | ||
{{ | * {{UCSC gene info|BIN1}} | ||
{{PDB Gallery|geneid=274}} | |||
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{{Adaptor proteins}} | |||
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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.[1][2][3]
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.[4]
Isoforms that are expressed in muscle and ubiquitously expressed isoforms localize to the cytoplasm and nucleus and activate a caspase-independent apoptotic process.[4]
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.[4]
Clinical significance
In humans, mutations in BIN1 have been associated with skeletal myopathies including centronuclear myopathy causing muscle weakness[3] and myotonic dystrophy causing progressive muscle wasting, myotonia, cataracts, and heart conduction defects.[5] An association has also been found between BIN1 mutations and Alzheimer's disease.[5] Knockdown of BIN1 in produces a cardiomyopathy phenotype in zebrafish,[6] and in sheep BIN1 may be responsible for the loss of T-tubules seen in heart failure.[7]
Interactions
BIN1 has been shown to interact with Phospholipase D1,[8] SNX4[9] and PLD2.[8]
References
- ↑ 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.
- ↑ 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.
- ↑ 3.0 3.1 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.
- ↑ 4.0 4.1 4.2 "Entrez Gene: BIN1 bridging integrator 1".
- ↑ 5.0 5.1 Prokic, Ivana; Cowling, Belinda S.; Laporte, Jocelyn (May 2014). "Amphiphysin 2 (BIN1) in physiology and diseases". Journal of Molecular Medicine (Berlin, Germany). 92 (5): 453–463. doi:10.1007/s00109-014-1138-1. ISSN 1432-1440. PMID 24590001.
- ↑ Hong, Ting-Ting; Smyth, James W.; Chu, Kevin Y.; Vogan, Jacob M.; Fong, Tina S.; Jensen, Brian C.; Fang, Kun; Halushka, Marc K.; Russell, Stuart D. (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.
- ↑ Caldwell, Jessica L.; Smith, Charlotte E. R.; Taylor, Rebecca F.; Kitmitto, Ashraf; Eisner, David A.; Dibb, Katharine M.; Trafford, Andrew W. (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.
- ↑ 8.0 8.1 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. UNITED STATES. 275 (25): 18751–8. doi:10.1074/jbc.M001695200. ISSN 0021-9258. PMID 10764771.
- ↑ Leprince, Corinne; 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. England. 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.
- 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.
- 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. 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. 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.
- 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.
- 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. doi:10.1073/pnas.96.16.8907. PMC 17706. PMID 10430869.
External links
- Human BIN1 genome location and BIN1 gene details page in the UCSC Genome Browser.
 | This article on a gene on human chromosome 2 is a stub. You can help Wikipedia by expanding it. |