Publication Date:
2002-08-17
Description:
In striated muscle, the plasma membrane forms tubular invaginations (transverse tubules or T-tubules) that function in depolarization-contraction coupling. Caveolin-3 and amphiphysin were implicated in their biogenesis. Amphiphysin isoforms have a putative role in membrane deformation at endocytic sites. An isoform of amphiphysin 2 concentrated at T-tubules induced tubular plasma membrane invaginations when expressed in nonmuscle cells. This property required exon 10, a phosphoinositide-binding module. In developing myotubes, amphiphysin 2 and caveolin-3 segregated in tubular and vesicular portions of the T-tubule system, respectively. These findings support a role of the bilayer-deforming properties of amphiphysin at T-tubules and, more generally, a physiological role of amphiphysin in membrane deformation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, Eunkyung -- Marcucci, Melissa -- Daniell, Laurie -- Pypaert, Marc -- Weisz, Ora A -- Ochoa, Gian-Carlo -- Farsad, Khashayar -- Wenk, Markus R -- De Camilli, Pietro -- CA46128/CA/NCI NIH HHS/ -- NS36251/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2002 Aug 16;297(5584):1193-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Howard Hughes Medical Institute, Yale University School of Medicine, 295 Congress Avenue, New Haven, CT 06510, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12183633" target="_blank"〉PubMed〈/a〉
Keywords:
Animals
;
CHO Cells
;
Caveolin 3
;
Caveolins/metabolism
;
Cell Differentiation
;
Cell Line
;
Cell Membrane/metabolism
;
Cell Membrane Structures/metabolism/*ultrastructure
;
Cricetinae
;
Dynamins
;
Exons
;
GTP Phosphohydrolases/metabolism
;
Liposomes/metabolism
;
Mice
;
Microscopy, Electron
;
Morphogenesis
;
*Muscle Development
;
Muscle, Skeletal/metabolism/*ultrastructure
;
Nerve Tissue Proteins/chemistry/genetics/*metabolism
;
Phosphatidylinositol 4,5-Diphosphate/metabolism
;
Protein Isoforms
;
Protein Structure, Tertiary
;
RNA, Small Interfering
;
RNA, Untranslated/metabolism
;
Recombinant Fusion Proteins/metabolism
;
Transfection
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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