Formation of stacked ER cisternae by low affinity protein interactions. (Articolo in rivista)

Type
Label
  • Formation of stacked ER cisternae by low affinity protein interactions. (Articolo in rivista) (literal)
Anno
  • 2003-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1083/jcb.200306020 (literal)
Alternative label
  • Snapp EL, Hegde RS, Francolini M, Lombardo F, Colombo S, Pedrazzini E, Borgese N, Lippincott-Schwartz J. (2003)
    Formation of stacked ER cisternae by low affinity protein interactions.
    in The Journal of cell biology
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Snapp EL, Hegde RS, Francolini M, Lombardo F, Colombo S, Pedrazzini E, Borgese N, Lippincott-Schwartz J. (literal)
Pagina inizio
  • 257 (literal)
Pagina fine
  • 269 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
  • http://jcb.rupress.org/content/163/2/257.full (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 163 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#note
  • IF 12,52 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 2 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • SEL, HRS, L-SJ: Cell Biology and Metabolism Branch, National Institutes of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892 BN: Consiglio Nazionale delle Ricerche Institute of Neuroscience, Cellular and Molecular Pharmacology Section FM, LF, CS: Department of Medical Pharmacology, University of Milan, 20129 Milano, Italy PE: Consiglio Nazionale delle Ricerche Istituto Biologia e Biotecnologia Agraria, 20133 Milano, Italy BN: Department of Pharmacobiology, University of Catanzaro, 88021 Roccelletta di Borgia, Catanzaro, Italy (literal)
Titolo
  • Formation of stacked ER cisternae by low affinity protein interactions. (literal)
Abstract
  • The endoplasmic reticulum (ER) can transform from a network of branching tubules into stacked membrane arrays (termed organized smooth ER [OSER]) in response to elevated levels of specific resident proteins, such as cytochrome b(5). Here, we have tagged OSER-inducing proteins with green fluorescent protein (GFP) to study OSER biogenesis and dynamics in living cells. Overexpression of these proteins induced formation of karmellae, whorls, and crystalloid OSER structures. Photobleaching experiments revealed that OSER-inducing proteins were highly mobile within OSER structures and could exchange between OSER structures and surrounding reticular ER. This indicated that binding interactions between proteins on apposing stacked membranes of OSER structures were not of high affinity. Addition of GFP, which undergoes low affinity, antiparallel dimerization, to the cytoplasmic domains of non–OSERinducing resident ER proteins was sufficient to induce OSER structures when overexpressed, but addition of a nondimerizing GFP variant was not. These results point to a molecular mechanism for OSER biogenesis that involves weak homotypic interactions between cytoplasmic domains of proteins. This mechanism may underlie the formation of other stacked membrane structures within cells. (literal)
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