Document Detail


Native structure and arrangement of inositol-1,4,5-trisphosphate receptor molecules in bovine cerebellar Purkinje cells as studied by quick-freeze deep-etch electron microscopy.
MedLine Citation:
PMID:  8890158     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
We used quick-freeze deep-etch replica electron microscopy to visualize the native structure of inositol-1,4,5-trisphosphate receptor (IP3R) in the cell. In the dendrites of Purkinje neurons of bovine cerebellum there were many vesicular organelles whose surfaces were covered with a two-dimensional crystalline array of molecules. Detailed examination of the cytoplasmic true surface of such vesicles in replica revealed that the structural unit, identified as IP3R by immunocytochemistry and subsequent Fourier analysis, is a square-shaped assembly and is aligned so that the side of the square is inclined by approximately 20 degrees from the row-line of the lattice. Comparison with the ryanodine receptor (RyaR), another intracellular Ca2+ channel on the endoplasmic reticulum, suggested that IP3R, unlike RyaR, has a very compact structure, potentially reflecting the crucial difference in the function of the cytoplasmic portion of the molecule.
Authors:
E Katayama; H Funahashi; T Michikawa; T Shiraishi; T Ikemoto; M Iino; K Mikoshiba
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The EMBO journal     Volume:  15     ISSN:  0261-4189     ISO Abbreviation:  EMBO J.     Publication Date:  1996 Sep 
Date Detail:
Created Date:  1996-12-10     Completed Date:  1996-12-10     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  8208664     Medline TA:  EMBO J     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  4844-51     Citation Subset:  IM    
Affiliation:
Department of Fine Morphology, Institute of Medical Science, The University of Tokyo, Bunkyo-ku, Japan.
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MeSH Terms
Descriptor/Qualifier:
Animals
Calcium Channels / metabolism,  ultrastructure*
Calmodulin-Binding Proteins / metabolism,  ultrastructure
Cattle
Cryopreservation
Inositol 1,4,5-Trisphosphate / metabolism*
Inositol 1,4,5-Trisphosphate Receptors
Microscopy, Electron
Muscle Proteins / metabolism,  ultrastructure
Purkinje Cells / metabolism,  ultrastructure*
Receptors, Cytoplasmic and Nuclear / metabolism,  ultrastructure*
Ryanodine Receptor Calcium Release Channel
Tissue Distribution
Chemical
Reg. No./Substance:
0/Calcium Channels; 0/Calmodulin-Binding Proteins; 0/Inositol 1,4,5-Trisphosphate Receptors; 0/Muscle Proteins; 0/Receptors, Cytoplasmic and Nuclear; 0/Ryanodine Receptor Calcium Release Channel; 85166-31-0/Inositol 1,4,5-Trisphosphate
Comments/Corrections
Erratum In:
EMBO J 1996 Dec 16;15(24):7188

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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