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Cloning of human erythroid dematin reveals another member of the villin family.

ABSTRACT: Dematin is an actin-bundling protein originally identified in the human erythroid membrane skeleton. Its actin-bundling activity is abolished upon phosphorylation by the cAMP-dependent protein kinase and is restored after dephosphorylation. Here we report the complete primary structure of human erythroid dematin, whose sequence includes a homologue of the "headpiece" sequence found at the C terminus of villin. This headpiece is essential for villin function in inducing microvillar development and actin redistribution. The widespread expression of dematin transcripts in human tissues suggests that dematin and its homologues may substitute for villin in villin-negative tissues to regulate actin reorganization by a phosphorylation-regulated mechanism.

SUBMITTER: Rana AP

PROVIDER: S-EPMC46990 | biostudies-other | 1993 Jul

REPOSITORIES: biostudies-other

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Cloning of human erythroid dematin reveals another member of the villin family.

Rana A P AP Ruff P P Maalouf G J GJ Speicher D W DW Chishti A H AH

Proceedings of the National Academy of Sciences of the United States of America 19930701 14

Dematin is an actin-bundling protein originally identified in the human erythroid membrane skeleton. Its actin-bundling activity is abolished upon phosphorylation by the cAMP-dependent protein kinase and is restored after dephosphorylation. Here we report the complete primary structure of human erythroid dematin, whose sequence includes a homologue of the "headpiece" sequence found at the C terminus of villin. This headpiece is essential for villin function in inducing microvillar development an ...[more]

PMID: 8341682

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