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{{ | '''Alpha-adducin''' is a [[protein]] that in humans is encoded by the ''ADD1'' [[gene]].<ref name="pmid1840603">{{cite journal | vauthors = Joshi R, Gilligan DM, Otto E, McLaughlin T, Bennett V | title = Primary structure and domain organization of human alpha and beta adducin | journal = J Cell Biol | volume = 115 | issue = 3 | pages = 665–75 |date=Nov 1991| pmid = 1840603 | pmc = 2289184 | doi =10.1083/jcb.115.3.665 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ADD1 adducin 1 (alpha)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=118| accessdate = }}</ref> | ||
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| section_title = | | section_title = | ||
| summary_text = | | summary_text = [[Adducin]]s are a family of [[cytoskeleton]] proteins encoded by three genes (alpha, beta, gamma). Adducin is a [[heterodimeric]] protein that consists of related subunits, which are produced from distinct genes but share a similar structure. Alpha- and beta-adducin include a [[protease]]-resistant [[N-terminal]] region and a protease-sensitive, [[hydrophilic]] [[C-terminal]] region. Alpha- and gamma-adducins are [[ubiquitous]]ly expressed. In contrast, beta-adducin is expressed at high levels in brain and [[hematopoietic]] tissues. Adducin binds with high affinity to Ca(2+)/[[calmodulin]] and is a [[substrate (biochemistry)|substrate]] for [[protein kinase]]s A and C. Alternative [[Protein splicing|splicing]] results in multiple variants encoding distinct [[isoforms]]; however, not all variants have been fully described. [[Polymorphism (biology)|Polymorphism]] in ADD1 is associated with [[hypertension]].<ref name="entrez" /> | ||
}} | }} | ||
==References== | ==References== | ||
{{reflist| | {{reflist}} | ||
==External links== | |||
* {{UCSC gene info|ADD1}} | |||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
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| citations = | | citations = | ||
*{{cite journal | author=Mangeat PH |title=Interaction of biological membranes with the cytoskeletal framework of living cells | *{{cite journal | author=Mangeat PH |title=Interaction of biological membranes with the cytoskeletal framework of living cells |journal=Biol. Cell |volume=64 |issue= 3 |pages= 261–81 |year= 1989 |pmid= 2976282 |doi=10.1016/0248-4900(88)90001-9 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Matsuoka Y, Li X, Bennett V |title=Adducin: structure, function and regulation |journal=Cell. Mol. Life Sci. |volume=57 |issue= 6 |pages= 884–95 |year= 2000 |pmid= 10950304 |doi=10.1007/PL00000731 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Goldberg YP, Lin BY, Andrew SE |title=Cloning and mapping of the alpha-adducin gene close to D4S95 and assessment of its relationship to Huntington disease |journal=Hum. Mol. Genet. |volume=1 |issue= 9 |pages= 669–75 |year= 1993 |pmid= 1284592 |doi=10.1093/hmg/1.9.669 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Taylor SA, Snell RG, Buckler A |title=Cloning of the alpha-adducin gene from the Huntington's disease candidate region of chromosome 4 by exon amplification |journal=Nat. Genet. |volume=2 |issue= 3 |pages= 223–7 |year= 1994 |pmid= 1345173 |doi= 10.1038/ng1192-223 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Gardner K, Bennett V |title=Modulation of spectrin-actin assembly by erythrocyte adducin |journal=Nature |volume=328 |issue= 6128 |pages= 359–62 |year= 1987 |pmid= 3600811 |doi= 10.1038/328359a0 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Gilligan DM, Lieman J, Bennett V |title=Assignment of the human beta-adducin gene (ADD2) to 2p13-p14 by in situ hybridization |journal=Genomics |volume=28 |issue= 3 |pages= 610–2 |year= 1996 |pmid= 7490111 |doi= 10.1006/geno.1995.1205 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Lin B, Nasir J, McDonald H |title=Genomic organization of the human alpha-adducin gene and its alternately spliced isoforms |journal=Genomics |volume=25 |issue= 1 |pages= 93–9 |year= 1995 |pmid= 7774961 |doi=10.1016/0888-7543(95)80113-Z |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Nasir J, Lin B, Bucan M |title=The murine homologues of the Huntington disease gene (Hdh) and the alpha-adducin gene (Add1) map to mouse chromosome 5 within a region of conserved synteny with human chromosome 4p16.3 |journal=Genomics |volume=22 |issue= 1 |pages= 198–201 |year= 1994 |pmid= 7959767 |doi= 10.1006/geno.1994.1361 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Kuhlman PA, Hughes CA, Bennett V, Fowler VM |title=A new function for adducin. Calcium/calmodulin-regulated capping of the barbed ends of actin filaments |journal=J. Biol. Chem. |volume=271 |issue= 14 |pages= 7986–91 |year= 1996 |pmid= 8626479 |doi= 10.1074/jbc.271.14.7986}} | ||
*{{cite journal | | *{{cite journal | vauthors=Li X, Bennett V |title=Identification of the spectrin subunit and domains required for formation of spectrin/adducin/actin complexes |journal=J. Biol. Chem. |volume=271 |issue= 26 |pages= 15695–702 |year= 1996 |pmid= 8663089 |doi=10.1074/jbc.271.26.15695 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Matsuoka Y, Hughes CA, Bennett V |title=Adducin regulation. Definition of the calmodulin-binding domain and sites of phosphorylation by protein kinases A and C |journal=J. Biol. Chem. |volume=271 |issue= 41 |pages= 25157–66 |year= 1996 |pmid= 8810272 |doi=10.1074/jbc.271.41.25157 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Hadano S, Ishida Y, Tomiyasu H |title=Transcript map of the human chromosome 4p16.3 consisting of 627 cDNA clones derived from 1 Mb of the Huntington's disease locus |journal=DNA Res. |volume=3 |issue= 4 |pages= 239–55 |year= 1997 |pmid= 8946164 |doi=10.1093/dnares/3.4.239 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Cusi D, Barlassina C, Azzani T |title=Polymorphisms of alpha-adducin and salt sensitivity in patients with essential hypertension |journal=Lancet |volume=349 |issue= 9062 |pages= 1353–7 |year= 1997 |pmid= 9149697 |doi=10.1016/S0140-6736(97)01029-5 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Kamitani A, Wong ZY, Fraser R |title=Human alpha-adducin gene, blood pressure, and sodium metabolism |journal=Hypertension |volume=32 |issue= 1 |pages= 138–43 |year= 1998 |pmid= 9674650 |doi=10.1161/01.HYP.32.1.138 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Matsuoka Y, Li X, Bennett V |title=Adducin is an in vivo substrate for protein kinase C: phosphorylation in the MARCKS-related domain inhibits activity in promoting spectrin-actin complexes and occurs in many cells, including dendritic spines of neurons |journal=J. Cell Biol. |volume=142 |issue= 2 |pages= 485–97 |year= 1998 |pmid= 9679146 |doi=10.1083/jcb.142.2.485 | pmc=2133059 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Fukata Y, Oshiro N, Kinoshita N |title=Phosphorylation of adducin by Rho-kinase plays a crucial role in cell motility |journal=J. Cell Biol. |volume=145 |issue= 2 |pages= 347–61 |year= 1999 |pmid= 10209029 |doi=10.1083/jcb.145.2.347 | pmc=2133101 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Halushka MK, Fan JB, Bentley K |title=Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis |journal=Nat. Genet. |volume=22 |issue= 3 |pages= 239–47 |year= 1999 |pmid= 10391210 |doi= 10.1038/10297 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Ferrandi M, Salardi S, Tripodi G |title=Evidence for an interaction between adducin and Na(+)-K(+)-ATPase: relation to genetic hypertension |journal=Am. J. Physiol. |volume=277 |issue= 4 Pt 2 |pages= H1338–49 |year= 1999 |pmid= 10516168 |doi= |display-authors=etal}} | ||
}} | }} | ||
{{refend}} | {{refend}} | ||
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Latest revision as of 01:41, 27 October 2017
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| External IDs | GeneCards: [1] | ||||||
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| Species | Human | Mouse | |||||
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| Location (UCSC) | n/a | n/a | |||||
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| Wikidata | |||||||
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Alpha-adducin is a protein that in humans is encoded by the ADD1 gene.[1][2]
Adducins are a family of cytoskeleton proteins encoded by three genes (alpha, beta, gamma). Adducin is a heterodimeric protein that consists of related subunits, which are produced from distinct genes but share a similar structure. Alpha- and beta-adducin include a protease-resistant N-terminal region and a protease-sensitive, hydrophilic C-terminal region. Alpha- and gamma-adducins are ubiquitously expressed. In contrast, beta-adducin is expressed at high levels in brain and hematopoietic tissues. Adducin binds with high affinity to Ca(2+)/calmodulin and is a substrate for protein kinases A and C. Alternative splicing results in multiple variants encoding distinct isoforms; however, not all variants have been fully described. Polymorphism in ADD1 is associated with hypertension.[2]
References
- ↑ Joshi R, Gilligan DM, Otto E, McLaughlin T, Bennett V (Nov 1991). "Primary structure and domain organization of human alpha and beta adducin". J Cell Biol. 115 (3): 665–75. doi:10.1083/jcb.115.3.665. PMC 2289184. PMID 1840603.
- ↑ 2.0 2.1 "Entrez Gene: ADD1 adducin 1 (alpha)".
External links
- Human ADD1 genome location and ADD1 gene details page in the UCSC Genome Browser.
Further reading
- Mangeat PH (1989). "Interaction of biological membranes with the cytoskeletal framework of living cells". Biol. Cell. 64 (3): 261–81. doi:10.1016/0248-4900(88)90001-9. PMID 2976282.
- Matsuoka Y, Li X, Bennett V (2000). "Adducin: structure, function and regulation". Cell. Mol. Life Sci. 57 (6): 884–95. doi:10.1007/PL00000731. PMID 10950304.
- Goldberg YP, Lin BY, Andrew SE, et al. (1993). "Cloning and mapping of the alpha-adducin gene close to D4S95 and assessment of its relationship to Huntington disease". Hum. Mol. Genet. 1 (9): 669–75. doi:10.1093/hmg/1.9.669. PMID 1284592.
- Taylor SA, Snell RG, Buckler A, et al. (1994). "Cloning of the alpha-adducin gene from the Huntington's disease candidate region of chromosome 4 by exon amplification". Nat. Genet. 2 (3): 223–7. doi:10.1038/ng1192-223. PMID 1345173.
- Gardner K, Bennett V (1987). "Modulation of spectrin-actin assembly by erythrocyte adducin". Nature. 328 (6128): 359–62. doi:10.1038/328359a0. PMID 3600811.
- Gilligan DM, Lieman J, Bennett V (1996). "Assignment of the human beta-adducin gene (ADD2) to 2p13-p14 by in situ hybridization". Genomics. 28 (3): 610–2. doi:10.1006/geno.1995.1205. PMID 7490111.
- Lin B, Nasir J, McDonald H, et al. (1995). "Genomic organization of the human alpha-adducin gene and its alternately spliced isoforms". Genomics. 25 (1): 93–9. doi:10.1016/0888-7543(95)80113-Z. PMID 7774961.
- Nasir J, Lin B, Bucan M, et al. (1994). "The murine homologues of the Huntington disease gene (Hdh) and the alpha-adducin gene (Add1) map to mouse chromosome 5 within a region of conserved synteny with human chromosome 4p16.3". Genomics. 22 (1): 198–201. doi:10.1006/geno.1994.1361. PMID 7959767.
- Kuhlman PA, Hughes CA, Bennett V, Fowler VM (1996). "A new function for adducin. Calcium/calmodulin-regulated capping of the barbed ends of actin filaments". J. Biol. Chem. 271 (14): 7986–91. doi:10.1074/jbc.271.14.7986. PMID 8626479.
- Li X, Bennett V (1996). "Identification of the spectrin subunit and domains required for formation of spectrin/adducin/actin complexes". J. Biol. Chem. 271 (26): 15695–702. doi:10.1074/jbc.271.26.15695. PMID 8663089.
- Matsuoka Y, Hughes CA, Bennett V (1996). "Adducin regulation. Definition of the calmodulin-binding domain and sites of phosphorylation by protein kinases A and C". J. Biol. Chem. 271 (41): 25157–66. doi:10.1074/jbc.271.41.25157. PMID 8810272.
- Hadano S, Ishida Y, Tomiyasu H, et al. (1997). "Transcript map of the human chromosome 4p16.3 consisting of 627 cDNA clones derived from 1 Mb of the Huntington's disease locus". DNA Res. 3 (4): 239–55. doi:10.1093/dnares/3.4.239. PMID 8946164.
- Cusi D, Barlassina C, Azzani T, et al. (1997). "Polymorphisms of alpha-adducin and salt sensitivity in patients with essential hypertension". Lancet. 349 (9062): 1353–7. doi:10.1016/S0140-6736(97)01029-5. PMID 9149697.
- Kamitani A, Wong ZY, Fraser R, et al. (1998). "Human alpha-adducin gene, blood pressure, and sodium metabolism". Hypertension. 32 (1): 138–43. doi:10.1161/01.HYP.32.1.138. PMID 9674650.
- Matsuoka Y, Li X, Bennett V (1998). "Adducin is an in vivo substrate for protein kinase C: phosphorylation in the MARCKS-related domain inhibits activity in promoting spectrin-actin complexes and occurs in many cells, including dendritic spines of neurons". J. Cell Biol. 142 (2): 485–97. doi:10.1083/jcb.142.2.485. PMC 2133059. PMID 9679146.
- Fukata Y, Oshiro N, Kinoshita N, et al. (1999). "Phosphorylation of adducin by Rho-kinase plays a crucial role in cell motility". J. Cell Biol. 145 (2): 347–61. doi:10.1083/jcb.145.2.347. PMC 2133101. PMID 10209029.
- Halushka MK, Fan JB, Bentley K, et al. (1999). "Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis". Nat. Genet. 22 (3): 239–47. doi:10.1038/10297. PMID 10391210.
- Ferrandi M, Salardi S, Tripodi G, et al. (1999). "Evidence for an interaction between adducin and Na(+)-K(+)-ATPase: relation to genetic hypertension". Am. J. Physiol. 277 (4 Pt 2): H1338–49. PMID 10516168.
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