Temporal differences in the appearance of NEP-B78 and an LBR-like protein during Xenopus nuclear envelope reassembly reflect the ordered recruitment of functionally discrete vesicle types.

2.50
Hdl Handle:
http://hdl.handle.net/10541/91350
Title:
Temporal differences in the appearance of NEP-B78 and an LBR-like protein during Xenopus nuclear envelope reassembly reflect the ordered recruitment of functionally discrete vesicle types.
Authors:
Drummond, Sheona P; Ferrigno, Paul; Lyon, Carol; Murphy, Jackie; Goldberg, Martin W; Allen, Terence D; Smythe, Carl; Hutchison, Christopher J
Abstract:
In this work, we have used novel mAbs against two proteins of the endoplasmic reticulum and outer nuclear membrane, termed NEP-B78 and p65, in addition to a polyclonal antibody against the inner nuclear membrane protein LBR (lamin B receptor), to study the order and dynamics of NE reassembly in the Xenopus cell-free system. Using these reagents, we demonstrate differences in the timing of recruitment of their cognate membrane proteins to the surface of decondensing chromatin in both the cell-free system and XLK-2 cells. We show unequivocally that, in the cell-free system, two functionally and biochemically distinct vesicle types are necessary for NE assembly. We find that the process of distinct vesicle recruitment to chromatin is an ordered one and that NEP-B78 defines a vesicle population involved in the earliest events of reassembly in this system. Finally, we present evidence that NEP-B78 may be required for the targeting of these vesicles to the surface of decondensing chromatin in this system. The results have important implications for the understanding of the mechanisms of nuclear envelope disassembly and reassembly during mitosis and for the development of systems to identify novel molecules that control these processes.
Affiliation:
MRC Protein Phosphorylation Unit, University of Dundee, Dundee DD1 4HN, Scotland, United Kingdom.
Citation:
Temporal differences in the appearance of NEP-B78 and an LBR-like protein during Xenopus nuclear envelope reassembly reflect the ordered recruitment of functionally discrete vesicle types. 1999, 144 (2):225-40 J. Cell Biol.
Journal:
The Journal of Cell Biology
Issue Date:
25-Jan-1999
URI:
http://hdl.handle.net/10541/91350
PubMed ID:
9922450
Type:
Article
Language:
en
ISSN:
0021-9525
Appears in Collections:
All Paterson Institute for Cancer Research

Full metadata record

DC FieldValue Language
dc.contributor.authorDrummond, Sheona Pen
dc.contributor.authorFerrigno, Paulen
dc.contributor.authorLyon, Carolen
dc.contributor.authorMurphy, Jackieen
dc.contributor.authorGoldberg, Martin Wen
dc.contributor.authorAllen, Terence Den
dc.contributor.authorSmythe, Carlen
dc.contributor.authorHutchison, Christopher Jen
dc.date.accessioned2010-02-08T11:21:28Z-
dc.date.available2010-02-08T11:21:28Z-
dc.date.issued1999-01-25-
dc.identifier.citationTemporal differences in the appearance of NEP-B78 and an LBR-like protein during Xenopus nuclear envelope reassembly reflect the ordered recruitment of functionally discrete vesicle types. 1999, 144 (2):225-40 J. Cell Biol.en
dc.identifier.issn0021-9525-
dc.identifier.pmid9922450-
dc.identifier.urihttp://hdl.handle.net/10541/91350-
dc.description.abstractIn this work, we have used novel mAbs against two proteins of the endoplasmic reticulum and outer nuclear membrane, termed NEP-B78 and p65, in addition to a polyclonal antibody against the inner nuclear membrane protein LBR (lamin B receptor), to study the order and dynamics of NE reassembly in the Xenopus cell-free system. Using these reagents, we demonstrate differences in the timing of recruitment of their cognate membrane proteins to the surface of decondensing chromatin in both the cell-free system and XLK-2 cells. We show unequivocally that, in the cell-free system, two functionally and biochemically distinct vesicle types are necessary for NE assembly. We find that the process of distinct vesicle recruitment to chromatin is an ordered one and that NEP-B78 defines a vesicle population involved in the earliest events of reassembly in this system. Finally, we present evidence that NEP-B78 may be required for the targeting of these vesicles to the surface of decondensing chromatin in this system. The results have important implications for the understanding of the mechanisms of nuclear envelope disassembly and reassembly during mitosis and for the development of systems to identify novel molecules that control these processes.en
dc.language.isoenen
dc.subject.meshAnimals-
dc.subject.meshAntibodies, Monoclonal-
dc.subject.meshCell-Free System-
dc.subject.meshChromatin-
dc.subject.meshEndoplasmic Reticulum-
dc.subject.meshFemale-
dc.subject.meshMice-
dc.subject.meshMice, Inbred BALB C-
dc.subject.meshNuclear Envelope-
dc.subject.meshNuclear Proteins-
dc.subject.meshRabbits-
dc.subject.meshReceptors, Cytoplasmic and Nuclear-
dc.subject.meshXenopus-
dc.titleTemporal differences in the appearance of NEP-B78 and an LBR-like protein during Xenopus nuclear envelope reassembly reflect the ordered recruitment of functionally discrete vesicle types.en
dc.typeArticleen
dc.contributor.departmentMRC Protein Phosphorylation Unit, University of Dundee, Dundee DD1 4HN, Scotland, United Kingdom.en
dc.identifier.journalThe Journal of Cell Biologyen
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