Source:http://linkedlifedata.com/resource/pubmed/id/17895372
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 20
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pubmed:dateCreated |
2007-10-11
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pubmed:abstractText |
The 3F3A monoclonal antibody to autocrine motility factor receptor (AMFR) labels mitochondria-associated smooth endoplasmic reticulum (ER) tubules. siRNA down-regulation of AMFR expression reduces mitochondria-associated 3F3A labelling. The 3F3A-labelled ER domain does not overlap with reticulon-labelled ER tubules, the nuclear membrane or perinuclear ER markers and only partially overlaps with the translocon component Sec61alpha. Upon overexpression of FLAG-tagged AMFR, 3F3A labelling is mitochondria associated, excluded from the perinuclear ER and co-distributes with reticulon. 3F3A labelling therefore defines a distinct mitochondria-associated ER domain. Elevation of free cytosolic Ca(2+) levels with ionomycin promotes dissociation of 3F3A-labelled tubules from mitochondria and, judged by electron microscopy, disrupts close contacts (<50 nm) between smooth ER tubules and mitochondria. The ER tubule-mitochondria association is similarly disrupted upon thapsigargin-induced release of ER Ca(2+) stores or purinergic receptor stimulation by ATP. The inositol (1,4,5)-trisphosphate [Ins(1,4,5)P(3)] receptor (IP3R) colocalises to 3F3A-labelled mitochondria-associated ER tubules, and conditions that induce ER tubule-mitochondria dissociation disrupt continuity between 3F3A- and IP3R-labelled ER domains. RAS-transformed NIH-3T3 cells have increased basal cytosolic Ca(2+) levels and show dissociation of the 3F3A-labelled, but not IP3R-labelled, ER from mitochondria. Our data indicate that regulation of the ER-mitochondria association by free cytosolic Ca(2+) is a characteristic of smooth ER domains and that multiple mechanisms regulate the interaction between these organelles.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amfr protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Ionomycin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Autocrine Motility Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytokine,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9533
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
120
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3553-64
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:17895372-Animals,
pubmed-meshheading:17895372-Antibodies, Monoclonal,
pubmed-meshheading:17895372-Calcium,
pubmed-meshheading:17895372-Calcium Signaling,
pubmed-meshheading:17895372-Cell Line,
pubmed-meshheading:17895372-Dogs,
pubmed-meshheading:17895372-Endoplasmic Reticulum, Smooth,
pubmed-meshheading:17895372-Ionomycin,
pubmed-meshheading:17895372-Mice,
pubmed-meshheading:17895372-Microscopy, Electron, Transmission,
pubmed-meshheading:17895372-Mitochondria,
pubmed-meshheading:17895372-NIH 3T3 Cells,
pubmed-meshheading:17895372-Receptors, Autocrine Motility Factor,
pubmed-meshheading:17895372-Receptors, Cytokine,
pubmed-meshheading:17895372-Ubiquitin-Protein Ligases
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pubmed:year |
2007
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pubmed:articleTitle |
Reversible interactions between smooth domains of the endoplasmic reticulum and mitochondria are regulated by physiological cytosolic Ca2+ levels.
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pubmed:affiliation |
Department of Cellular and Physiological Sciences, Life Sciences Institute, University of British Columbia, Vancouver V6T 1Z3, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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