Biology:Annexin A2
 Generic protein structure example |
Annexin A2 also known as annexin II is a protein that in humans is encoded by the ANXA2 gene.[1]
Annexin 2 is involved in diverse cellular processes such as cell motility (especially that of the epithelial cells), linkage of membrane-associated protein complexes to the actin cytoskeleton, endocytosis, fibrinolysis, ion channel formation, and cell matrix interactions. It is a calcium-dependent phospholipid-binding protein whose function is to help organize exocytosis of intracellular proteins to the extracellular domain. Annexin II is a pleiotropic protein meaning that its function is dependent on place and time in the body.
Gene
The ANXA2 gene, located at 15q22.2, has three pseudogenes located on chromosomes 4, 9 and 10, respectively. Multiple alternatively spliced transcript variants encoding different isoforms have been found for this gene.[2]
Function
This protein is a member of the annexin family. Members of this calcium-dependent phospholipid-binding protein family play a role in the regulation of cellular growth and in signal transduction pathways. This protein functions as an autocrine factor which heightens osteoclast formation and bone resorption.[2] Epigenetic regulation of Annexin A2 has been identified as a key determinant of mesenchymal transformation in brain tumors.[3] Maternal deficiency of the ANXA2 gene contributes to shallow decidual invasion by placental cytotrophoblast cells. These findings highlight the maternal contribution to the pathogenesis of severe preeclampsia.[4]
Annexin A2 has been proposed to function inside the cell in sorting of endosomes and outside the cell in anticoagulant reactions.
Interactions
Annexin A2 has been shown to interact with Prohibitin,[5] CEACAM1,[6] S100A10,[7][8] PCNA,[9] complement Factor H,[10] and a number of viral factors including the HPV16 minor capsid protein L2.[11][12]
See also
References
- ↑ "Cloning and identification of annexin II as an autocrine/paracrine factor that increases osteoclast formation and bone resorption". The Journal of Biological Chemistry 269 (46): 28696–28701. November 1994. doi:10.1016/S0021-9258(19)61961-7. PMID 7961821.
- ↑ 2.0 2.1 "Entrez Gene: ANXA2 annexin A2". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=302.
- ↑ "Integrative Modeling Reveals Annexin A2-mediated Epigenetic Control of Mesenchymal Glioblastoma". eBioMedicine 12: 72–85. October 2016. doi:10.1016/j.ebiom.2016.08.050. PMID 27667176.
- ↑ "Endometrial Decidualization: The Primary Driver of Pregnancy Health". International Journal of Molecular Sciences 21 (11): 4092. June 2020. doi:10.3390/ijms21114092. PMID 32521725.
- ↑ "Prohibitin and prohibitone are contained in high-molecular weight complexes and interact with alpha-actinin and annexin A2". Biochimie 84 (12): 1207–1220. December 2002. doi:10.1016/S0300-9084(02)00027-5. PMID 12628297.
- ↑ "CEACAM1, a cell-cell adhesion molecule, directly associates with annexin II in a three-dimensional model of mammary morphogenesis". The Journal of Biological Chemistry 278 (50): 50338–50345. December 2003. doi:10.1074/jbc.M309115200. PMID 14522961.
- ↑ "The crystal structure of a complex of p11 with the annexin II N-terminal peptide". Nature Structural Biology 6 (1): 89–95. January 1999. doi:10.1038/4965. PMID 9886297.
- ↑ "Endothelial cell annexin A2 regulates polyubiquitination and degradation of its binding partner S100A10/p11". The Journal of Biological Chemistry 283 (28): 19192–19200. July 2008. doi:10.1074/jbc.M800100200. PMID 18434302.
- ↑ "A proteomics approach to identify proliferating cell nuclear antigen (PCNA)-binding proteins in human cell lysates. Identification of the human CHL12/RFCs2-5 complex as a novel PCNA-binding protein". The Journal of Biological Chemistry 277 (43): 40362–40367. October 2002. doi:10.1074/jbc.M206194200. PMID 12171929.
- ↑ "Annexin-II, DNA, and histones serve as factor H ligands on the surface of apoptotic cells". The Journal of Biological Chemistry 285 (6): 3766–3776. February 2010. doi:10.1074/jbc.M109.045427. PMID 19951950.
- ↑ "The S100A10 subunit of the annexin A2 heterotetramer facilitates L2-mediated human papillomavirus infection". PLOS ONE 7 (8): e43519. 2012. doi:10.1371/journal.pone.0043519. PMID 22927980. Bibcode: 2012PLoSO...743519W.
- ↑ "Inhibition of Langerhans cell maturation by human papillomavirus type 16: a novel role for the annexin A2 heterotetramer in immune suppression". Journal of Immunology 192 (10): 4748–4757. May 2014. doi:10.4049/jimmunol.1303190. PMID 24719459.
Further reading
- "S100A10, annexin A2, and annexin a2 heterotetramer as candidate plasminogen receptors". Frontiers in Bioscience 10 (1–3): 300–325. January 2005. doi:10.2741/1529. PMID 15574370.
- "Regulation of ecto-5'-nucleotidase activity via Ca2+-dependent, annexin 2-mediated membrane rearrangement?". Biochemical Society Transactions 34 (Pt 3): 374–376. June 2006. doi:10.1042/BST0340374. PMID 16709165.
- "Annexin II inhibits calcium-dependent phospholipase A1 and lysophospholipase but not triacyl glycerol lipase activities of rat liver hepatic lipase". FEBS Letters 296 (3): 237–240. January 1992. doi:10.1016/0014-5793(92)80294-Q. PMID 1531641.
- "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". The Journal of Infection 24 (3): 317–320. May 1992. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151.
- "The protein-tyrosine kinase substrate, calpactin I heavy chain (p36), is part of the primer recognition protein complex that interacts with DNA polymerase alpha". The Journal of Biological Chemistry 266 (8): 5169–5176. March 1991. doi:10.1016/S0021-9258(19)67770-7. PMID 1825830.
- "Characterization of the cell-cycle-regulated protein calcyclin from Ehrlich ascites tumor cells. Identification of two binding proteins obtained by Ca2(+)-dependent affinity chromatography". European Journal of Biochemistry 195 (3): 795–800. February 1991. doi:10.1111/j.1432-1033.1991.tb15768.x. PMID 1999197.
- "Protein-protein recognition via short amphiphilic helices; a mutational analysis of the binding site of annexin II for p11". The EMBO Journal 9 (13): 4207–4213. December 1990. doi:10.1002/j.1460-2075.1990.tb07868.x. PMID 2148288.
- "Characterization of the human lipocortin-2-encoding multigene family: its structure suggests the existence of a short amino acid unit undergoing duplication". Gene 95 (2): 243–251. November 1990. doi:10.1016/0378-1119(90)90367-Z. PMID 2174397.
- "A discontinuous epitope on p36, the major substrate of src tyrosine-protein-kinase, brings the phosphorylation site into the neighbourhood of a consensus sequence for Ca2+/lipid-binding proteins". FEBS Letters 236 (1): 201–204. August 1988. doi:10.1016/0014-5793(88)80314-4. PMID 2456953.
- "The protein-tyrosine kinase substrate p36 is also a substrate for protein kinase C in vitro and in vivo". Molecular and Cellular Biology 6 (7): 2738–2744. July 1986. doi:10.1128/mcb.6.7.2738. PMID 2946940.
- "Chromosomal localization of the human genes for lipocortin I and lipocortin II". Oncogene Research 2 (4): 299–310. May 1988. PMID 2969496.
- "Two human 35 kd inhibitors of phospholipase A2 are related to substrates of pp60v-src and of the epidermal growth factor receptor/kinase". Cell 46 (2): 191–199. July 1986. doi:10.1016/0092-8674(86)90736-1. PMID 3013422.
- "A complex of Grb2 adaptor protein, Sos exchange factor, and a 36-kDa membrane-bound tyrosine phosphoprotein is implicated in ras activation in T cells". The Journal of Biological Chemistry 269 (12): 9019–9023. March 1994. doi:10.1016/S0021-9258(17)37070-9. PMID 7510700.
- "Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C". The Journal of Cell Biology 126 (2): 539–548. July 1994. doi:10.1083/jcb.126.2.539. PMID 7518469.
- "Construction of a human full-length cDNA bank". Gene 150 (2): 243–250. December 1994. doi:10.1016/0378-1119(94)90433-2. PMID 7821789.
- "Regional localization of human chromosome 15 loci". Genomics 23 (3): 619–627. October 1994. doi:10.1006/geno.1994.1550. PMID 7851890.
- "Cloning and identification of annexin II as an autocrine/paracrine factor that increases osteoclast formation and bone resorption". The Journal of Biological Chemistry 269 (46): 28696–28701. November 1994. doi:10.1016/S0021-9258(19)61961-7. PMID 7961821.
- "Identification and characterization of alpha-protein kinase C binding proteins in normal and transformed REF52 cells". Biochemistry 33 (5): 1223–1228. February 1994. doi:10.1021/bi00171a023. PMID 8110754.
- "An endothelial cell-surface form of annexin II binds human cytomegalovirus". Biochemical and Biophysical Research Communications 198 (3): 983–989. February 1994. doi:10.1006/bbrc.1994.1140. PMID 8117306.
- "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–174. January 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
External links
- Annexin+A2 at the US National Library of Medicine Medical Subject Headings (MeSH)
- Human ANXA2 genome location and ANXA2 gene details page in the UCSC Genome Browser.
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