Literature DB >> 3136784

Plasmalemmal undercoat: the cytoskeleton supporting the plasmalemma.

H Ishikawa1.   

Abstract

The plasmalemmal undercoat can be defined as the electron-dense material of layered organization closely applied to the cytoplasmic surface of the plasma membrane (plasmalemma) as revealed by thin-section electron microscopy. Though the structures which fulfill this criterion occur widely, most of them have not received the attention they may deserve. The undercoat is a special form of the cytoskeleton-membrane interaction, though it constitutes a part of the cytoskeleton. The significance of the plasmalemmal undercoat may be primarily to provide a structural support for the membrane. With this support, cells can perform many important functions on their limited or whole surfaces. The undercoat may provide a mechanical support to the plasmalemma so that the membrane may acquire rigidity, strength and elasticity. Through association with the membrane, the undercoat may regulate the distribution of integral membrane proteins to form and maintain various functional domains on the plasmalemma. The undercoat may further provide attachment sites for cytoskeletal fibrous components such as actin filaments, intermediate filaments and microtubules.

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Year:  1988        PMID: 3136784     DOI: 10.1679/aohc.51.127

Source DB:  PubMed          Journal:  Arch Histol Cytol        ISSN: 0914-9465


  7 in total

1.  Polymerization of actin in RBL-2H3 cells can be triggered through either the IgE receptor or the adenosine receptor but different signaling pathways are used.

Authors:  J R Apgar
Journal:  Mol Biol Cell       Date:  1994-03       Impact factor: 4.138

2.  Plectin tethers desmin intermediate filaments onto subsarcolemmal dense plaques containing dystrophin and vinculin.

Authors:  Takao Hijikata; Tohru Murakami; Harunori Ishikawa; Hiroshi Yorifuji
Journal:  Histochem Cell Biol       Date:  2003-01-18       Impact factor: 4.304

3.  Co-distribution of annexin VI and actin in secretory ameloblasts and odontoblasts of rat incisor.

Authors:  M Goldberg; J Feinberg; S Lecolle; M A Kaetzel; D Rainteau; J L Lessard; J R Dedman; S Weinman
Journal:  Cell Tissue Res       Date:  1991-01       Impact factor: 5.249

4.  Activation of protein kinase C in rat basophilic leukemia cells stimulates increased production of phosphatidylinositol 4-phosphate and phosphatidylinositol 4,5-bisphosphate: correlation with actin polymerization.

Authors:  J R Apgar
Journal:  Mol Biol Cell       Date:  1995-01       Impact factor: 4.138

5.  Evidence for a direct, nucleotide-sensitive interaction between actin and liver cell membranes.

Authors:  M P Tranter; S P Sugrue; M A Schwartz
Journal:  J Cell Biol       Date:  1989-12       Impact factor: 10.539

6.  Binding of actin to liver cell membranes: the state of membrane-bound actin.

Authors:  M P Tranter; S P Sugrue; M A Schwartz
Journal:  J Cell Biol       Date:  1991-03       Impact factor: 10.539

7.  Confocal laser microscopy of dystrophin localization in guinea pig skeletal muscle fibers.

Authors:  T Masuda; N Fujimaki; E Ozawa; H Ishikawa
Journal:  J Cell Biol       Date:  1992-11       Impact factor: 10.539

  7 in total

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