ADD1

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Adducin 1 (alpha)

Identifiers

Symbols

ADD1; ADDA; MGC3339; MGC44427

External IDs

OMIM: 102680 MGI: 87918 HomoloGene: 22758 GeneCards: ADD1 Gene

Gene Ontology
Molecular function	• actin binding • calmodulin binding • transcription factor binding • spectrin binding • protein homodimerization activity • metal ion binding • protein heterodimerization activity • actin filament binding
Cellular component	• nucleus • cytoplasm • cytosol • cytoskeleton • plasma membrane • F-actin capping protein complex
Biological process	• apoptosis • cellular component disassembly involved in apoptosis • actin cytoskeleton organization • positive regulation of protein binding • barbed-end actin filament capping • actin filament bundle assembly
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 4:
2.85 – 2.93 Mb

Chr 5:
34.92 – 34.97 Mb

PubMed search

[1]

[2]

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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2289184.
^ ^a ^b "Entrez Gene: ADD1 adducin 1 (alpha)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=118.

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. 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2133059.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2133101.
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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