Cloning of human erythroid dematin reveals another member of the villin family.
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.
Rana
A P
AP
Department of Biomedical Research, St. Elizabeth's Hospital, Tufts University School of Medicine, Boston, MA 02135.
Ruff
P
P
Maalouf
G J
GJ
Speicher
D W
DW
Chishti
A H
AH
D000199:Actins / Q000378:metabolism; D000595:Amino Acid Sequence; D001483:Base Sequence; D001798:Blood Proteins / Q000235:genetics* / Q000378:metabolism; D002352:Carrier Proteins / Q000235:genetics; D015723:Gene Library; D006801:Humans; D008565:Membrane Proteins / Q000235:genetics*; D008840:Microfilament Proteins / Q000235:genetics; D008969:Molecular Sequence Data; D005810:Multigene Family / Q000235:genetics*; D010750:Phosphoproteins; D012333:RNA, Messenger / Q000235:genetics; D015183:Restriction Mapping; D012156:Reticulocytes / Q000502:physiology*; D017386:Sequence Homology, Amino Acid
D000199:Actins; D001798:Blood Proteins; D002352:Carrier Proteins; C044805:DMTN protein, human; D008565:Membrane Proteins; D008840:Microfilament Proteins; D010750:Phosphoproteins; D012333:RNA, Messenger; C026615:villin