Document Detail


The role of multifunctional M1 metallopeptidases in cell cycle progression.
MedLine Citation:
PMID:  21258033     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
BACKGROUND: Metallopeptidases of the M1 family are found in all phyla (except viruses) and are important in the cell cycle and normal growth and development. M1s often have spatiotemporal expression patterns which allow for strict regulation of activity. Mutations in the genes encoding M1s result in disease and are often lethal. This family of zinc metallopeptidases all share the catalytic region containing a signature amino acid exopeptidase (GXMXN) and a zinc binding (HEXXH[18X]E) motif. In addition, M1 aminopeptidases often also contain additional membrane association and/or protein interaction motifs. These protein interaction domains may function independently of M1 enzymatic activity and can contribute to multifunctionality of the proteins.
SCOPE: A brief review of M1 metalloproteases in plants and animals and their roles in the cell cycle is presented. In animals, human puromycin-sensitive aminopeptidase (PSA) acts during mitosis and perhaps meiosis, while the insect homologue puromycin-sensitive aminopeptidase (PAM-1) is required for meiotic and mitotic exit; the remaining human M1 family members appear to play a direct or indirect role in mitosis/cell proliferation. In plants, meiotic prophase aminopeptidase 1 (MPA1) is essential for the first steps in meiosis, and aminopeptidase M1 (APM1) appears to be important in mitosis and cell division.
CONCLUSIONS: M1 metalloprotease activity in the cell cycle is conserved across phyla. The activities of the multifunctional M1s, processing small peptides and peptide hormones and contributing to protein trafficking and signal transduction processes, either directly or indirectly impact on the cell cycle. Identification of peptide substrates and interacting protein partners is required to understand M1 function in fertility and normal growth and development in plants.
Authors:
Wendy Ann Peer
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Review     Date:  2011-01-21
Journal Detail:
Title:  Annals of botany     Volume:  107     ISSN:  1095-8290     ISO Abbreviation:  Ann. Bot.     Publication Date:  2011 May 
Date Detail:
Created Date:  2011-05-11     Completed Date:  2011-08-30     Revised Date:  2013-06-30    
Medline Journal Info:
Nlm Unique ID:  0372347     Medline TA:  Ann Bot     Country:  England    
Other Details:
Languages:  eng     Pagination:  1171-81     Citation Subset:  IM    
Affiliation:
Department of Horticulture and Landscape Architecture, 625 Agriculture Mall Drive, Purdue University, West Lafayette, IN 47907 USA. peerw@purdue.edu
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MeSH Terms
Descriptor/Qualifier:
Animals
Cell Cycle*
Humans
Metalloproteases / chemistry,  genetics,  metabolism*
Models, Biological
Plant Cells
Plants / enzymology
Chemical
Reg. No./Substance:
EC 3.4.-/Metalloproteases
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