Membrane bound members of the M1 family: More than aminopeptidases

Anthony L. Albiston, Siying Ye, Yeen Chai Siew

Research output: Contribution to journalReview ArticleResearchpeer-review

63 Citations (Scopus)

Abstract

In mammals the M1 aminopeptidase family consists of nine different proteins, five of which are integral membrane proteins. The aminopeptidases are defined by two motifs in the catalytic domain; a zinc binding motif HEXXH-(X18)-E and an exopeptidase motif GXMEN. Aminopeptidases of this family are able to cleave a broad range of peptides down to only to a single peptide. This ability to either generate or degrade active peptide hormones is the focus of this review. In addition to their capacity to degrade a range of peptides a number of these aminopeptidases have novel functions that impact on cell signalling and will be discussed.

Original languageEnglish
Pages (from-to)491-500
Number of pages10
JournalProtein and Peptide Letters
Volume11
Issue number5
DOIs
Publication statusPublished - 1 Oct 2004
Externally publishedYes

Keywords

  • Aminopeptidase
  • Angiotensin IV
  • APA
  • APN
  • ERAAP
  • IRAP
  • TRH-DE

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