Mitochondrial Band-7 family proteins: scaffolds for respiratory chain assembly?

Research output: Contribution to journalReview ArticleScientificpeer-review

Researchers

Research units

  • Univ Oxford, University of Oxford, Dept Plant Sci
  • University of Oxford

Abstract

The band-7 protein family comprises a diverse set of membrane-bound proteins characterized by the presence of a conserved domain. The exact function of this band-7 domain remains elusive, but examples from animal and bacterial stomatin-type proteins demonstrate binding to lipids and the ability to assemble into membrane-bound oligomers that form putative scaffolds. Some members, such as prohibitins (PHB) and human stomatin-like protein 2 (HsSLP2), localize to the mitochondrial inner membrane where they function in cristae formation and hyperfusion. In Arabidopsis, the band-7 protein family has diversified and includes plant-specific members. Mitochondrial-localized members include prohibitins (AtPHBs) and two stomatin-like proteins (AtSLP1 and -2). Studies into PHB function in plants have demonstrated an involvement in root meristem proliferation and putative scaffold formation for mAAA proteases, but it remains unknown how these roles are achieved at the molecular level. In this minireview we summarize the current status of band-7 protein functions in Arabidopsis, and speculate how the mitochondrial members might recruit specific lipids to form microdomains that could shape the organization and functioning of the respiratory chain.

Details

Original languageEnglish
Article number141
Number of pages6
JournalFRONTIERS IN PLANT SCIENCE
Volume5
Publication statusPublished - 8 Apr 2014
MoE publication typeA2 Review article in a scientific journal

    Research areas

  • plant mitochondria, respiratory chain, protein complexes, band-7 protein family, cardiolipin, microdomains, STOMATIN-LIKE PROTEIN-2, SENSING ION CHANNELS, ARABIDOPSIS-THALIANA, PLASMA-MEMBRANE, AAA PROTEASES, SACCHAROMYCES-CEREVISIAE, CELL-PROLIFERATION, PLANT-MITOCHONDRIA, SPFH DOMAIN, COMPLEX I

ID: 36172206