Membrane bound members of the M1 family: more than aminopeptidases |
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Authors: | Albiston Anthony L Ye Siying Chai Siew Yeen |
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Affiliation: | Howard Florey Institute of Experimental Physiology and Medicine, University of Melbourne, Parkville, 3010 Australia. albist@hfi.unimelb.edu.au |
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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. |
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