scholarly journals The inner nuclear membrane proteins Man1 and Ima1 link to two different types of chromatin at the nuclear periphery inS. pombe

Nucleus ◽  
2012 ◽  
Vol 3 (1) ◽  
pp. 77-87 ◽  
Author(s):  
Babett Steglich ◽  
Guillaume Filion ◽  
Bas van Steensel ◽  
Karl Ekwall
Keyword(s):  
Membrane Proteins ◽  
Nuclear Membrane ◽  
Nuclear Periphery ◽  
Inner Nuclear Membrane ◽  
Different Types

scholarly journals Lamin-dependent Localization of UNC-84, A Protein Required for Nuclear Migration in Caenorhabditis elegans

2002 ◽  
Vol 13 (3) ◽  
pp. 892-901 ◽  
Author(s):  
Kenneth K. Lee ◽  
Daniel Starr ◽  
Merav Cohen ◽  
Jun Liu ◽  
Min Han ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Membrane Proteins ◽  
Nuclear Envelope ◽  
Nuclear Membrane ◽  
Nuclear Periphery ◽  
Nuclear Migration ◽  
Cell Stage ◽  
Inner Nuclear Membrane ◽  
Late Anaphase

Mutations in the Caenorhabditis elegans unc-84 gene cause defects in nuclear migration and anchoring. We show that endogenous UNC-84 protein colocalizes with Ce-lamin at the nuclear envelope and that the envelope localization of UNC-84 requires Ce-lamin. We also show that during mitosis, UNC-84 remains at the nuclear periphery until late anaphase, similar to known inner nuclear membrane proteins. UNC-84 protein is first detected at the 26-cell stage and thereafter is present in most cells during development and in adults. UNC-84 is properly expressed in unc-83 andanc-1 lines, which have phenotypes similar tounc-84, suggesting that neither the expression nor nuclear envelope localization of UNC-84 depends on UNC-83 or ANC-1 proteins. The envelope localization of Ce-lamin, Ce-emerin, Ce-MAN1, and nucleoporins are unaffected by the loss of UNC-84. UNC-84 is not required for centrosome attachment to the nucleus because centrosomes are localized normally in unc-84 hyp7 cells despite a nuclear migration defect. Models for UNC-84 localization are discussed.

scholarly journals Structural Characterization of the LEM Motif Common to Three Human Inner Nuclear Membrane Proteins

Structure ◽  
2001 ◽  
Vol 9 (6) ◽  
pp. 503-511 ◽  
Author(s):  
Cédric Laguri ◽  
Bernard Gilquin ◽  
Nicolas Wolff ◽  
Régine Romi-Lebrun ◽  
Karine Courchay ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Structural Characterization ◽  
Nuclear Membrane ◽  
Inner Nuclear Membrane

scholarly journals Integral membrane proteins specific to the inner nuclear membrane and associated with the nuclear lamina.

1988 ◽  
Vol 107 (6) ◽  
pp. 2029-2036 ◽  
Author(s):  
A Senior ◽  
L Gerace
Keyword(s):  
Membrane Proteins ◽  
Nuclear Membrane ◽  
Immunofluorescence Microscopy ◽  
Nuclear Lamina ◽  
Integral Membrane Proteins ◽  
Inner Nuclear Membrane ◽  
Attachment Sites ◽  
Nonionic Detergent ◽  
Pore Complexes ◽  
Integral Proteins

We obtained a monoclonal antibody (RL13) that identifies three integral membrane proteins specific to the nuclear envelope of rat liver, a major 75-kD polypeptide and two more minor components of 68 and 55 kD. Immunogold labeling of isolated nuclear envelopes demonstrates that these antigens are localized specifically to the inner nuclear membrane, and that the RL13 epitope occurs on the inner membrane's nucleoplasmic surface where the nuclear lamina is found. When nuclear envelopes are extracted with solutions containing nonionic detergent and high salt to solubilize nuclear membranes and pore complexes, most of these integral proteins remain associated with the insoluble lamina. Since the polypeptides recognized by RL13 are relatively abundant, they may function as lamina attachment sites in the inner nuclear membrane. Major cross-reacting antigens are found by immunoblotting and immunofluorescence microscopy in all rat cells examined. Therefore, these integral proteins are biochemical markers for the inner nuclear membrane and will be useful models for studying nuclear membrane biogenesis.

Inner nuclear membrane proteins: impact on human disease

Chromosoma ◽  
2012 ◽  
Vol 121 (2) ◽  
pp. 153-167 ◽  
Author(s):  
Iván Méndez-López ◽  
Howard J. Worman
Keyword(s):  
Membrane Proteins ◽  
Nuclear Membrane ◽  
Human Disease ◽  
Inner Nuclear Membrane

Nesprin isoforms: are they inside or outside the nucleus?

2010 ◽  
Vol 38 (1) ◽  
pp. 278-280 ◽  
Author(s):  
Glenn E. Morris ◽  
K. Natalie Randles
Keyword(s):  
Membrane Proteins ◽  
Experimental Evidence ◽  
Nuclear Membrane ◽  
Nuclear Import ◽  
Nuclear Lamina ◽  
Cellular Organization ◽  
Inner Nuclear Membrane

The giant isoforms of nesprins 1 and 2 are emerging as important players in cellular organization, particularly in the positioning of nuclei, and possibly other organelles, within the cytoplasm. The experimental evidence suggests that nesprins also occur at the inner nuclear membrane, where they interact with the nuclear lamina. In this paper, we consider whether this is consistent with current ideas about nesprin anchorage and about mechanisms for nuclear import of membrane proteins.

scholarly journals RanGTPase regulates the interaction between the inner nuclear membrane proteins, Samp1 and Emerin

2018 ◽  
Vol 1860 (6) ◽  
pp. 1326-1334 ◽  
Author(s):  
Balaje Vijayaraghavan ◽  
Ricardo A. Figueroa ◽  
Cecilia Bergqvist ◽  
Amit J. Gupta ◽  
Paulo Sousa ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Nuclear Membrane ◽  
Inner Nuclear Membrane
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