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HSPA9
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Mitochondrial 70kDa heat shock protein (mtHsp70), also known as mortalin, is a protein that in humans is encoded by the HSPA9 gene.[5][6]
Function
[edit]The product encoded by this gene belongs to the heat shock protein 70 family which contains both heat-inducible and constitutively expressed members. The latter are called heat-shock cognate proteins. This gene encodes a heat-shock cognate protein. This protein plays a role in the control of cell proliferation. It may also act as a chaperone.[6]
Interactions
[edit]Clinical relevance and genetic deficiency
[edit]In 2015, a group around Andrea Superti-Furga showed that biallelic variants in the HSPA9 gene may result in a combination of congenital malformations called the EVEN-PLUS syndrome.[9][10] These genetic variants have been shown to interfere with normal HSPA9 function [11]
References
[edit]- ^ a b c GRCh38: Ensembl release 89: ENSG00000113013 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000024359 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Domanico SZ, DeNagel DC, Dahlseid JN, Green JM, Pierce SK (Jun 1993). "Cloning of the gene encoding peptide-binding protein 74 shows that it is a new member of the heat shock protein 70 family". Mol Cell Biol. 13 (6): 3598–610. doi:10.1128/mcb.13.6.3598. PMC 359829. PMID 7684501.
- ^ a b "Entrez Gene: HSPA9 heat shock 70kDa protein 9 (mortalin)".
- ^ Mizukoshi E, Suzuki M, Loupatov A, Uruno T, Hayashi H, Misono T, Kaul SC, Wadhwa R, Imamura T (Oct 1999). "Fibroblast growth factor-1 interacts with the glucose-regulated protein GRP75/mortalin". Biochem. J. 343 (2): 461–6. doi:10.1042/0264-6021:3430461. PMC 1220575. PMID 10510314.
- ^ Wadhwa R, Yaguchi T, Hasan MK, Mitsui Y, Reddel RR, Kaul SC (Apr 2002). "Hsp70 family member, mot-2/mthsp70/GRP75, binds to the cytoplasmic sequestration domain of the p53 protein". Exp. Cell Res. 274 (2): 246–53. doi:10.1006/excr.2002.5468. PMID 11900485.
- ^ Royer-Bertrand B, Castillo-Taucher S, Moreno-Salinas R, Cho TJ, Chae JH, Choi M, et al. (November 2015). "Mutations in the heat-shock protein A9 (HSPA9) gene cause the EVEN-PLUS syndrome of congenital malformations and skeletal dysplasia". Scientific Reports. 5 17154. Bibcode:2015NatSR...517154R. doi:10.1038/srep17154. PMC 4657157. PMID 26598328.
- ^ "MIM 616854: Even Plus Syndrome". OMIM.
- ^ Moseng MA, Nix JC, Page RC (April 2019). "Biophysical Consequences of EVEN-PLUS Syndrome Mutations for the Function of Mortalin". The Journal of Physical Chemistry B. 123 (16): 3383–3396. doi:10.1021/acs.jpcb.9b00071. PMC 6483861. PMID 30933555.
Further reading
[edit]- Kaul SC, Taira K, Pereira-Smith OM, Wadhwa R (2003). "Mortalin: present and prospective". Exp. Gerontol. 37 (10–11): 1157–64. doi:10.1016/S0531-5565(02)00135-3. PMID 12470827. S2CID 44450296.
- Yaguchi T, Aida S, Kaul SC, Wadhwa R (2007). "Involvement of mortalin in cellular senescence from the perspective of its mitochondrial import, chaperone, and oxidative stress management functions". Ann. N. Y. Acad. Sci. 1100 (1): 306–11. Bibcode:2007NYASA1100..306Y. doi:10.1196/annals.1395.032. PMID 17460192. S2CID 43848246.
- Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R (1993). "Human liver protein map: a reference database established by microsequencing and gel comparison". Electrophoresis. 13 (12): 992–1001. doi:10.1002/elps.11501301201. PMID 1286669. S2CID 23518983.
- Kaul SC, Wadhwa R, Matsuda Y, Hensler PJ, Pereira-Smith OM, Komatsu Y, Mitsui Y (1995). "Mouse and human chromosomal assignments of mortalin, a novel member of the murine hsp70 family of proteins". FEBS Lett. 361 (2–3): 269–72. Bibcode:1995FEBSL.361..269K. doi:10.1016/0014-5793(95)00177-B. PMID 7698336. S2CID 36957259.
- Bhattacharyya T, Karnezis AN, Murphy SP, Hoang T, Freeman BC, Phillips B, Morimoto RI (1995). "Cloning and subcellular localization of human mitochondrial hsp70". J. Biol. Chem. 270 (4): 1705–10. doi:10.1074/jbc.270.4.1705. PMID 7829505.
- Furlini G, Vignoli M, Re MC, Gibellini D, Ramazzotti E, Zauli G, La Placa M (1994). "Human immunodeficiency virus type 1 interaction with the membrane of CD4+ cells induces the synthesis and nuclear translocation of 70K heat shock protein". J. Gen. Virol. 75 (1): 193–9. doi:10.1099/0022-1317-75-1-193. PMID 7906708.
- Matoba R, Okubo K, Hori N, Fukushima A, Matsubara K (1994). "The addition of 5'-coding information to a 3'-directed cDNA library improves analysis of gene expression". Gene. 146 (2): 199–207. doi:10.1016/0378-1119(94)90293-3. PMID 8076819.
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Hughes GJ, Frutiger S, Paquet N, Pasquali C, Sanchez JC, Tissot JD, Bairoch A, Appel RD, Hochstrasser DF (1994). "Human liver protein map: update 1993". Electrophoresis. 14 (11): 1216–22. doi:10.1002/elps.11501401181. PMID 8313870. S2CID 33424554.
- Ji H, Reid GE, Moritz RL, Eddes JS, Burgess AW, Simpson RJ (1997). "A two-dimensional gel database of human colon carcinoma proteins". Electrophoresis. 18 (3–4): 605–13. doi:10.1002/elps.1150180344. PMID 9150948. S2CID 25454450.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- Mizukoshi E, Suzuki M, Loupatov A, Uruno T, Hayashi H, Misono T, Kaul SC, Wadhwa R, Imamura T (1999). "Fibroblast growth factor-1 interacts with the glucose-regulated protein GRP75/mortalin". Biochem. J. 343 (2): 461–6. doi:10.1042/0264-6021:3430461. PMC 1220575. PMID 10510314.
- O'Keeffe B, Fong Y, Chen D, Zhou S, Zhou Q (2000). "Requirement for a kinase-specific chaperone pathway in the production of a Cdk9/cyclin T1 heterodimer responsible for P-TEFb-mediated tat stimulation of HIV-1 transcription". J. Biol. Chem. 275 (1): 279–87. doi:10.1074/jbc.275.1.279. PMID 10617616.
- Kaula SC, Reddelb RR, Sugiharac T, Mitsuia Y, Wadhwac R (2000). "Inactivation of p53 and life span extension of human diploid fibroblasts by mot-2". FEBS Lett. 474 (2–3): 159–64. Bibcode:2000FEBSL.474..159K. doi:10.1016/S0014-5793(00)01594-5. PMID 10838077. S2CID 85853656.
- Agostini I, Popov S, Li J, Dubrovsky L, Hao T, Bukrinsky M (2000). "Heat-shock protein 70 can replace viral protein R of HIV-1 during nuclear import of the viral preintegration complex". Exp. Cell Res. 259 (2): 398–403. doi:10.1006/excr.2000.4992. PMID 10964507.
- Xie H, Hu Z, Chyna B, Horrigan SK, Westbrook CA (2001). "Human mortalin (HSPA9): a candidate for the myeloid leukemia tumor suppressor gene on 5q31". Leukemia. 14 (12): 2128–34. doi:10.1038/sj.leu.2401935. PMID 11187902.
- Andersen JS, Lyon CE, Fox AH, Leung AK, Lam YW, Steen H, Mann M, Lamond AI (2002). "Directed proteomic analysis of the human nucleolus". Curr. Biol. 12 (1): 1–11. Bibcode:2002CBio...12....1A. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298. S2CID 14132033.
- Carette J, Lehnert S, Chow TY (2002). "Implication of PBP74/mortalin/GRP75 in the radio-adaptive response". Int. J. Radiat. Biol. 78 (3): 183–90. doi:10.1080/09553000110097208. PMID 11869473. S2CID 536461.
- Wadhwa R, Yaguchi T, Hasan MK, Mitsui Y, Reddel RR, Kaul SC (2002). "Hsp70 family member, mot-2/mthsp70/GRP75, binds to the cytoplasmic sequestration domain of the p53 protein". Exp. Cell Res. 274 (2): 246–53. doi:10.1006/excr.2002.5468. PMID 11900485.
External links
[edit]- HSPA9+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- PDBe-KB provides an overview of all the structure information available in the PDB for Human Stress-70 protein, mitochondrial
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