アンフィファイシン、アンフィフィジン、アンフィフィシン
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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2016/04/28 07:16:19」(JST)
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Amphiphysin |
Rendering of 1KY7
|
Available structures |
PDB |
Ortholog search: PDBe, RCSB |
List of PDB id codes |
1KY7, 1UTC, 3SOG, 4ATM
|
|
|
Identifiers |
Symbols |
AMPH ; AMPH1 |
External IDs |
OMIM: 600418 MGI: 103574 HomoloGene: 121585 GeneCards: AMPH Gene |
Gene ontology |
Molecular function |
• protein binding
• phospholipid binding
|
Cellular component |
• synaptic vesicle
• actin cytoskeleton
• cell junction
• synaptic vesicle membrane
• leading edge membrane
|
Biological process |
• endocytosis
• synaptic transmission
• learning
• synaptic vesicle endocytosis
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Sources: Amigo / QuickGO |
|
RNA expression pattern |
|
More reference expression data |
Orthologs |
Species |
Human |
Mouse |
Entrez |
273 |
218038 |
Ensembl |
ENSG00000078053 |
ENSMUSG00000021314 |
UniProt |
P49418 |
Q7TQF7 |
RefSeq (mRNA) |
NM_001635 |
NM_001289546 |
RefSeq (protein) |
NP_001626 |
NP_001276475 |
Location (UCSC) |
Chr 7:
38.38 – 38.63 Mb |
Chr 13:
18.95 – 19.15 Mb |
PubMed search |
[1] |
[2] |
|
Amphiphysin is a protein that in humans is encoded by the AMPH gene.[1][2]
This gene encodes a protein associated with the cytoplasmic surface of synaptic vesicles. A subset of patients with stiff person syndrome who were also affected by breast cancer are positive for autoantibodies against this protein. Alternate splicing of this gene results in two transcript variants encoding different isoforms. Additional splice variants have been described, but their full length sequences have not been determined.[2]
Amphiphysin is a brain-enriched protein with an N-terminal lipid interaction, dimerisation and membrane bending BAR domain, a middle clathrin and adaptor binding domain and a C-terminal SH3 domain. In the brain, its primary function is thought to be the recruitment of dynamin to sites of clathrin-mediated endocytosis. There are 2 mammalian amphiphysins with similar overall structure. A ubiquitous splice form of amphiphysin 2 that does not contain clathrin or adaptor interactions is highly expressed in muscle tissue and is involved in the formation and stabilization of the T-tubule network. In other tissues amphiphysin is likely involved in other membrane bending and curvature stabilization events.
Contents
- 1 Interactions
- 2 See also
- 3 References
- 4 Further reading
- 5 External links
Interactions
Amphiphysin has been shown to interact with DNM1,[3][4][5][6][7] Phospholipase D1,[8] CDK5R1,[9] PLD2,[8] CABIN1[10] and SH3GL2.[3][11]
See also
References
- ^ De Camilli, P.; Thomas, A; Cofiell, R; Folli, F; Lichte, B; Piccolo, G; Meinck, HM; Austoni, M; et al. (December 1993). "The synaptic vesicle-associated protein amphiphysin is the 128-kD autoantigen of Stiff-Man syndrome with breast cancer". J Exp Med 178 (6): 2219–23. doi:10.1084/jem.178.6.2219. PMC 2191289. PMID 8245793.
- ^ a b "Entrez Gene: AMPH amphiphysin (Stiff-Man syndrome with breast cancer 128kDa autoantigen)".
- ^ a b Micheva, K. D.; Kay, BK; McPherson, PS (October 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; Doyle, CA; Owen, D; Hunt, SP; McMahon, HT (October 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.
- ^ McMahon, Harvey T; Wigge, Patrick; Smith, Corrin (August 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.
- ^ Chen-Hwang, M.-C.; Chen, HR; Elzinga, M; Hwang, YW (May 2002). "Dynamin is a minibrain kinase/dual specificity Yak1-related kinase 1A substrate". J. Biol. Chem. 277 (20): 17597–604. doi:10.1074/jbc.M111101200. PMID 11877424.
- ^ Grabs, D.; Slepnev, VI; Songyang, Z; David, C; Lynch, M; Cantley, LC; De Camilli, P (May 1997). "The SH3 domain of amphiphysin binds the proline-rich domain of dynamin at a single site that defines a new SH3 binding consensus sequence". J. Biol. Chem. 272 (20): 13419–25. doi:10.1074/jbc.272.20.13419. PMID 9148966.
- ^ a b Lee, C.; Kim, SR; Chung, JK; Frohman, MA; Kilimann, MW; Rhee, SG (June 2000). "Inhibition of phospholipase D by amphiphysins". J. Biol. Chem. 275 (25): 18751–8. doi:10.1074/jbc.M001695200. PMID 10764771.
- ^ Floyd, S. R.; Porro, EB; Slepnev, VI; Ochoa, GC; Tsai, LH; De Camilli, P (March 2001). "Amphiphysin 1 binds the cyclin-dependent kinase (cdk) 5 regulatory subunit p35 and is phosphorylated by cdk5 and cdc2". J. Biol. Chem. 276 (11): 8104–10. doi:10.1074/jbc.M008932200. PMID 11113134.
- ^ Lai, M. M.; Luo, HR; Burnett, PE; Hong, JJ; Snyder, SH (November 2000). "The calcineurin-binding protein cain is a negative regulator of synaptic vesicle endocytosis". J. Biol. Chem. 275 (44): 34017–20. doi:10.1074/jbc.C000429200. PMID 10931822.
- ^ Modregger, J.; Schmidt, AA; Ritter, B; Huttner, WB; Plomann, M (February 2003). "Characterization of Endophilin B1b, a brain-specific membrane-associated lysophosphatidic acid acyl transferase with properties distinct from endophilin A1". J. Biol. Chem. 278 (6): 4160–7. doi:10.1074/jbc.M208568200. PMID 12456676.
Further reading
- Lichte, B; Veh, RW; Meyer, HE; Kilimann, MW (1992). "Amphiphysin, a novel protein associated with synaptic vesicles". EMBO J. 11 (7): 2521–30. PMC 556727. PMID 1628617.
- Yamamoto, Raina; Li, Xu; Winter, Silke; Francke, Uta; Kilimann, Manfred W. (1995). "Primary structure of human amphiphysin, the dominant autoantigen of paraneoplastic stiff-man syndrome, and mapping of its gene (AMPH) to chromosome 7p13-p14". Hum. Mol. Genet. 4 (2): 265–8. doi:10.1093/hmg/4.2.265. PMID 7757077.
- David, C; Solimena, M; Decamilli, P (1994). "Autoimmunity in stiff-Man syndrome with breast cancer is targeted to the C-terminal region of human amphiphysin, a protein similar to the yeast proteins, Rvs167 and Rvs161". FEBS Lett. 351 (1): 73–9. doi:10.1016/0014-5793(94)00826-4. PMID 8076697.
- David, C.; McPherson, PS; Mundigl, O; De Camilli, P (1996). "A role of amphiphysin in synaptic vesicle endocytosis suggested by its binding to dynamin in nerve terminals". Proc. Natl. Acad. Sci. U.S.A. 93 (1): 331–5. doi:10.1073/pnas.93.1.331. PMC 40232. PMID 8552632.
- Grabs, D.; Slepnev, VI; Songyang, Z; David, C; Lynch, M; Cantley, LC; De Camilli, P (1997). "The SH3 domain of amphiphysin binds the proline-rich domain of dynamin at a single site that defines a new SH3 binding consensus sequence". J. Biol. Chem. 272 (20): 13419–25. doi:10.1074/jbc.272.20.13419. PMID 9148966.
- Butler, M. H.; David, C; Ochoa, GC; Freyberg, Z; Daniell, L; Grabs, D; Cremona, O; De Camilli, P (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, A. R.; 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.
- McMahon, Harvey T; Wigge, Patrick; Smith, Corrin (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, Kristina D.; Ramjaun, Antoine R.; Kay, Brian K.; McPherson, Peter S. (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.
- Wigge, P; Köhler, K; Vallis, Y; Doyle, CA; Owen, D; Hunt, SP; McMahon, HT (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.
- Floyd, S; Butler, MH; Cremona, O; David, C; Freyberg, Z; Zhang, X; Solimena, M; Tokunaga, A; et al. (1998). "Expression of amphiphysin I, an autoantigen of paraneoplastic neurological syndromes, in breast cancer". Mol. Med. 4 (1): 29–39. PMC 2230265. PMID 9513187.
- Ramjaun, Antoine R.; McPherson, Peter S. (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.
- Slepnev, V. I.; Ochoa, GC; Butler, MH; Grabs, D; De Camilli, P (1998). "Role of phosphorylation in regulation of the assembly of endocytic coat complexes". Science 281 (5378): 821–4. doi:10.1126/science.281.5378.821. PMID 9694653.
- Cestra, G.; Castagnoli, L; Dente, L; Minenkova, O; Petrelli, A; Migone, N; Hoffmüller, U; Schneider-Mergener, J; Cesareni, G (1999). "The SH3 domains of endophilin and amphiphysin bind to the proline-rich region of synaptojanin 1 at distinct sites that display an unconventional binding specificity". J. Biol. Chem. 274 (45): 32001–7. doi:10.1074/jbc.274.45.32001. PMID 10542231.
- Slepnev, V. I.; Ochoa, GC; Butler, MH; De Camilli, P (2000). "Tandem arrangement of the clathrin and AP-2 binding domains in amphiphysin 1 and disruption of clathrin coat function by amphiphysin fragments comprising these sites". J. Biol. Chem. 275 (23): 17583–9. doi:10.1074/jbc.M910430199. PMID 10748223.
- Lee, C.; Kim, SR; Chung, JK; Frohman, MA; Kilimann, MW; Rhee, SG (2000). "Inhibition of phospholipase D by amphiphysins". J. Biol. Chem. 275 (25): 18751–8. doi:10.1074/jbc.M001695200. PMID 10764771.
- Onofri, F.; Giovedi, S; Kao, HT; Valtorta, F; Bongiorno Borbone, L; De Camilli, P; Greengard, P; Benfenati, F (2000). "Specificity of the binding of synapsin I to Src homology 3 domains". J. Biol. Chem. 275 (38): 29857–67. doi:10.1074/jbc.M006018200. PMID 10899172.
- Lai, M. M.; Luo, HR; Burnett, PE; Hong, JJ; Snyder, SH (2000). "The calcineurin-binding protein cain is a negative regulator of synaptic vesicle endocytosis". J. Biol. Chem. 275 (44): 34017–20. doi:10.1074/jbc.C000429200. PMID 10931822.
- Floyd, S. R.; Porro, EB; Slepnev, VI; Ochoa, GC; Tsai, LH; De Camilli, P (2001). "Amphiphysin 1 binds the cyclin-dependent kinase (cdk) 5 regulatory subunit p35 and is phosphorylated by cdk5 and cdc2". J. Biol. Chem. 276 (11): 8104–10. doi:10.1074/jbc.M008932200. PMID 11113134.
- a. Leventis, Peter; m. Chow, Brenda; Stewart, Bryan A.; Iyengar, Balaji; Campos, Ana Regina; Boulianne, Gabrielle L. (2001). "Drosophila Amphiphysin is a post-synaptic protein required for normal locomotion but not endocytosis". Traffic. 2 (11): 839–50. doi:10.1034/j.1600-0854.2001.21113.x. PMID 11733051.
- Zhang, Bing; Zelhof, Andrew C. (2002). "Amphiphysins: raising the BAR for synaptic vesicle recycling and membrane dynamics". Traffic. 3 (7): 452–60. doi:10.1034/j.1600-0854.2002.30702.x. PMID 12047553. Review.
- Zelhof, AC; Bao, H; Hardy, RW; Razzaq, A; Zhang, B; Doe, CQ (2001). "Drosophila Amphiphysin is implicated in protein localization and membrane morphogenesis but not in synaptic vesicle endocytosis". Development 128 (24): 5005–15. PMID 11748137.
- Mathew, D; Popescu, A; Budnik, V (2003). "Drosophila amphiphysin functions during synaptic Fasciclin II membrane cycling". J Neurosci. 23 (33): 10710–6. PMID 14627656.
External links
- Bringing your curves to the bar, amphiphysin home page
- De Camilli, Pietro; Takei, Kohji; Slepnev, Vladimir I.; Haucke, Volker (May 1999). "Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis". Nat. Cell Biol. 1 (1): 33–9. doi:10.1038/9004. PMID 10559861.
- Peter, B. J.; Kent, HM; Mills, IG; Vallis, Y; Butler, PJ; Evans, PR; McMahon, HT (January 2004). "BAR domains as sensors of membrane curvature: the amphiphysin BAR structure". Science 303 (5657): 495–9. doi:10.1126/science.1092586. PMID 14645856.
- Evergren, Emma; Marcucci, Melissa; Tomilin, Nikolay; Löw, Peter; Slepnev, Vladimir; Andersson, Fredrik; Gad, Helge; Brodin, Lennart; et al. (July 2004). "Amphiphysin is a component of clathrin coats formed during synaptic vesicle recycling at the lamprey giant synapse". Traffic 5 (7): 514–28. doi:10.1111/j.1398-9219.2004.00198.x. PMID 15180828.
- Razzaq, A.; Robinson, IM; McMahon, HT; Skepper, JN; Su, Y; Zelhof, AC; Jackson, AP; Gay, NJ; O'Kane, CJ (November 2001). "Amphiphysin is necessary for organization of the excitation-contraction coupling machinery of muscles, but not for synaptic vesicle endocytosis in Drosophila". Genes Dev. 15 (22): 2967–79. doi:10.1101/gad.207801. PMC 312829. PMID 11711432.
UpToDate Contents
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English Journal
- Gene expression variance in hippocampal tissue of temporal lobe epilepsy patients corresponds to differential memory performance.
- Bungenberg J1, Surano N1, Grote A2, Surges R3, Pernhorst K1, Hofmann A4, Schoch S1, Helmstaedter C3, Becker AJ5.
- Neurobiology of disease.Neurobiol Dis.2016 Feb;86:121-30. doi: 10.1016/j.nbd.2015.11.011. Epub 2015 Nov 26.
- Temporal lobe epilepsy (TLE) is a severe brain disorder affecting particularly young adults. TLE is frequently associated with memory deterioration and neuronal damage of the hippocampal formation. It thereby reveals striking parallels to neurodegenerative disorders including Alzheimer's disease (AD
- PMID 26631617
- Possible regulation of caveolar endocytosis and flattening by phosphorylation of F-BAR domain protein PACSIN2/Syndapin II.
- Senju Y1, Suetsugu S2.
- Bioarchitecture.Bioarchitecture.2016 Jan 8:0. [Epub ahead of print]
- Caveolae are flask-shaped invaginations of the plasma membrane. The BAR domain proteins form crescent-shaped dimers, and their oligomeric filaments are considered to form spirals at the necks of invaginations, such as clathrin-coated pits and caveolae. PACSIN2/Syndapin II is one of the BAR domain-co
- PMID 26745030
- Phosphorylation regulates the endocytic function of the yeast dynamin-related protein Vps1.
- Smaczynska-de Rooij II1, Marklew CJ1, Allwood EG1, Palmer SE1, Booth WI1, Mishra R2, Goldberg MW2, Ayscough KR3.
- Molecular and cellular biology.Mol Cell Biol.2015 Dec 28. pii: MCB.00833-15. [Epub ahead of print]
- The family of dynamin proteins is known to function in many eukaryotic membrane fusion and fission events. The yeast dynamin-related protein Vps1 functions at several stages of membrane trafficking including Golgi to endosome and vacuole, peroxisomal fission, and endocytic scission. We have previous
- PMID 26711254
Japanese Journal
- 自己免疫性脳炎の広がりとその進歩(ワークショップ:神経疾患診療の進歩,2012年,第53回日本心身医学会総会ならびに学術講演会(鹿児島))
- 渡邊 修
- 心身医学 53(10), 913-920, 2013-10-01
- 多様な抗原に対する免疫応答によりさまざまな臨床的特徴を有する脳炎・脳症が引き起こされる.初発症状として,抑うつ,パーソナリティ障害,記憶障害,不眠,統合失調症様の症状を呈し,多くの症例で,頭部MRIや髄液所見が正常であることもあり,心身医療・精神医療の領域でもこれらの理解が重要である.近年,細胞膜表面抗原に対する自己抗体介在性脳炎が次々と見出されている.具体的には,グルタミン受容体(NMDA受容体 …
- NAID 110009657689
- Stiff-person症候群と自己抗体 (特集 Antibody Update)
- Sub-acute Demyelinating Polyradiculoneuropathy as an Initial Symptom of Peripheral T Cell Lymphoma, Not Otherwise Specified (PTCL-NOS)
- Kawanishi Kazunobu,Ohyama Yasuyo,Kanai Yoshitake,Hirase Tikara,Tanaka Hirokazu,Miyatake Junichi,Tatsumi Youichi,Ashida Takashi,Nakamine Hirokazu,Matsumura Itaru
- Internal Medicine 51(15), 2015-2020, 2012
- … Several antibodies relating to paraneoplastic syndrome such as Ma1, Ma2, Amphiphysin, CV2, Ri, Yo and Hu were all negative. …
- NAID 130002062269
Related Links
- Amphiphysin recruits dynamin to sites of endocytosis. Links to research on the mechanism of dynamin in vesicle scission and endocytosis. Research on proteins involved in clathrin-coated vesicle formation. Research on membrane ...
- カルパインによるタンパク質分解が関与するエンドサイトーシス制御機構モデル 本論文は、カルパインによるamphiphysin Iの分解が、神経過剰興奮時におけるシナプス小胞のエンドサイトーシスを抑制するというものです。
Related Pictures
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- 英
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- アンフィファイシン、アンフィフィジン
[★]
- 英
- amphiphysin
- 関
- アンフィファイシン、アンフィフィシン
[★]
- 英
- amphiphysin
- 関
- アンフィフィジン、アンフィフィシン