Major vault protein

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An Error has occurred retrieving Wikidata item for infobox Major vault protein, also known as lung resistance-related protein is a protein that in humans is encoded by the MVP gene.[1][2] 78 copies of the protein assemble into the large compartments called vaults.

Function

This gene encodes the major vault protein which is a lung infection resistance-related protein. Vaults are multi-subunit structures that may be involved in nucleo-cytoplasmic transport. Major vault protein comprises 70% of vaults which also contain vPARP and TEP1.[3] This protein mediates drug resistance, perhaps via a transport process. It is widely distributed in normal tissues and overexpressed in multidrug-resistant cancer cells. The protein overexpression is a potentially useful marker of clinical drug resistance. This gene produces two transcripts by using two alternative exon 2 sequences; however, the open reading frames are the same in both transcripts.[2]

Interactions

Major vault protein coimmunoprecipitates with the human estrogen receptor and treatment with estradiol increases major vault protein associated with the estrogen receptor in nuclear extracts.[4] Major vault protein has been shown to interact with estrogen receptor alpha,[5] PTEN[6] and PARP4.[7][8]

References

  1. Scheffer GL, Wijngaard PL, Flens MJ, Izquierdo MA, Slovak ML, Pinedo HM, et al. (June 1995). "The drug resistance-related protein LRP is the human major vault protein". Nature Medicine. 1 (6): 578–582. doi:10.1038/nm0695-578. hdl:20.500.11755/c49e6086-ede3-4b91-ac6e-4ab9158c6cac. PMID 7585126. S2CID 29771830.
  2. 2.0 2.1 "Entrez Gene: MVP major vault protein".
  3. Berger W, Steiner E, Grusch M, Elbling L, Micksche M (January 2009). "Vaults and the major vault protein: novel roles in signal pathway regulation and immunity". Cellular and Molecular Life Sciences. 66 (1): 43–61. doi:10.1007/s00018-008-8364-z. PMC 11131553. PMID 18759128.
  4. Kong LB, Siva AC, Rome LH, Stewart PL (April 1999). "Structure of the vault, a ubiquitous celular component". Structure. 7 (4): 371–379. doi:10.1016/s0969-2126(99)80050-1. PMID 10196123.
  5. Abbondanza C, Rossi V, Roscigno A, Gallo L, Belsito A, Piluso G, et al. (June 1998). "Interaction of vault particles with estrogen receptor in the MCF-7 breast cancer cell". The Journal of Cell Biology. 141 (6): 1301–1310. doi:10.1083/jcb.141.6.1301. PMC 2132791. PMID 9628887.
  6. Yu Z, Fotouhi-Ardakani N, Wu L, Maoui M, Wang S, Banville D, et al. (October 2002). "PTEN associates with the vault particles in HeLa cells". The Journal of Biological Chemistry. 277 (43): 40247–40252. doi:10.1074/jbc.M207608200. PMID 12177006.
  7. van Zon A, Mossink MH, Schoester M, Scheffer GL, Scheper RJ, Sonneveld P, et al. (March 2002). "Structural domains of vault proteins: a role for the coiled coil domain in vault assembly". Biochemical and Biophysical Research Communications. 291 (3): 535–541. doi:10.1006/bbrc.2002.6472. PMID 11855821.
  8. Kickhoefer VA, Siva AC, Kedersha NL, Inman EM, Ruland C, Streuli M, et al. (September 1999). "The 193-kD vault protein, VPARP, is a novel poly(ADP-ribose) polymerase". The Journal of Cell Biology. 146 (5): 917–928. doi:10.1083/jcb.146.5.917. PMC 2169495. PMID 10477748.

Further reading