F
IPR000163

Prohibitin

InterPro entry
Short nameProhibitin
Overlapping
homologous
superfamilies
 

Description

This entry describes proteins similar to prohibitin (a lipid raft-associated integral membrane protein). Individual proteins of the SPFH (band 7) domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes
[8]
. These microdomains, in addition to being stable scaffolds, may also be dynamic units with their own regulatory functions
[1, 6]
. Prohibitin is a mitochondrial inner-membrane protein which may act as a chaperone for the stabilization of mitochondrial proteins. Human prohibitin forms a hetero-oligomeric complex with Bap-37 (prohibitin 2, an SPFH domain carrying homologue). This complex may protect non-assembled membrane proteins against proteolysis by the m-AAA protease
[5, 7]
. Prohibitin and Bap-37 yeast homologues have been implicated in yeast longevity
[4]
and in the maintenance of mitochondrial morphology. Sequence comparisons suggest that the prohibitin gene is an analogue of Cc, a Drosophila melanogaster gene that is vital for normal development
[3]
.

Genes that negatively regulate proliferation inside the cell are of considerable interest because of the implications in processes such as development and cancer
[9]
. Prohibitin acts as a cytoplasmic anti-proliferative protein, is widely expressed in a variety of tissues and inhibits DNA synthesis. Studies have suggested that prohibitin may be a suppressor gene and is associated with tumour development and/or progression of at least some breast cancers
[2]
.

References

1.The SPFH domain: implicated in regulating targeted protein turnover in stomatins and other membrane-associated proteins. Tavernarakis N, Driscoll M, Kyrpides NC. Trends Biochem. Sci. 24, 425-7, (1999). View articlePMID: 10542406

2.The human prohibitin gene located on chromosome 17q21 is mutated in sporadic breast cancer. Sato T, Saito H, Swensen J, Olifant A, Wood C, Danner D, Sakamoto T, Takita K, Kasumi F, Miki Y. Cancer Res. 52, 1643-6, (1992). View articlePMID: 1540973

3.The role and therapeutic potential of prohibitin in disease. Theiss AL, Sitaraman SV. Biochim. Biophys. Acta 1813, 1137-43, (2011). View articlePMID: 21296110

4.Yeast replicative life span--the mitochondrial connection. Jazwinski SM. FEMS Yeast Res. 5, 119-25, (2004). View articlePMID: 15489194

5.AAA proteases of mitochondria: quality control of membrane proteins and regulatory functions during mitochondrial biogenesis. Langer T, Kaser M, Klanner C, Leonhard K. Biochem. Soc. Trans. 29, 431-6, (2001). View articlePMID: 11498003

6.Scaffolding microdomains and beyond: the function of reggie/flotillin proteins. Langhorst MF, Reuter A, Stuermer CA. Cell. Mol. Life Sci. 62, 2228-40, (2005). View articlePMID: 16091845

7.Prohibitins regulate membrane protein degradation by the m-AAA protease in mitochondria. Steglich G, Neupert W, Langer T. Mol. Cell. Biol. 19, 3435-42, (1999). PMID: 10207067

8.The SPFH domain-containing proteins: more than lipid raft markers. Browman DT, Hoegg MB, Robbins SM. Trends Cell Biol. 17, 394-402, (2007). View articlePMID: 17766116

9.Prohibitin, an evolutionarily conserved intracellular protein that blocks DNA synthesis in normal fibroblasts and HeLa cells. Nuell MJ, Stewart DA, Walker L, Friedman V, Wood CM, Owens GA, Smith JR, Schneider EL, Dell' Orco R, Lumpkin CK. Mol. Cell. Biol. 11, 1372-81, (1991). View articlePMID: 1996099

GO terms

biological process

  • None

molecular function

  • None

cellular component

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