Abstract
Periplakin regulates keratin organisation and participates in the assembly of epidermal cornified envelopes. A proteomic approach identified annexin A9 as a novel interacting partner for periplakin N-terminus. The presence of annexin A9 in complexes with periplakin was confirmed by immunoblotting of proteins immunoprecipitated by anti-HA or anti-annexin A9 antibodies. Both endogenous and GFP-tagged annexin A9 co-localise with endogenous periplakin and transfected periplakin N-terminus at MCF-7 cell borders and aggregate after Okadaic acid treatment. Annexin A9 and periplakin co-localise in the epidermis and annexin A9 is up-regulated in differentiating keratinocytes, but the epidermal annexin A9 expression does not require periplakin.
Copyright © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Annexins / chemistry
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Annexins / genetics
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Annexins / metabolism*
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Cell Differentiation
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Cell Line
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Cell Membrane / metabolism
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Cytoskeletal Proteins / chemistry
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Cytoskeletal Proteins / genetics
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Cytoskeletal Proteins / metabolism
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Epithelial Cells / metabolism
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Humans
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Keratinocytes / cytology
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Keratinocytes / metabolism
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MCF-7 Cells
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Mice
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Multiprotein Complexes / chemistry
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Multiprotein Complexes / genetics
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Multiprotein Complexes / metabolism
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Okadaic Acid / pharmacology
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Plakins / chemistry
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Plakins / genetics
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Plakins / metabolism*
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Proteomics
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
Substances
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ANXA9 protein, human
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Annexins
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Anxa9 protein, mouse
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Cytoskeletal Proteins
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Multiprotein Complexes
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PPL protein, human
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Plakins
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Ppl protein, mouse
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Recombinant Proteins
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Okadaic Acid