Nuclear membrane proteins at heart of muscle disorders

2013 ◽  
Author(s):  
Aisha El-Awady
Keyword(s):  
Membrane Proteins ◽  
Nuclear Membrane ◽  
Muscle Disorders

Sorting nuclear membrane proteins at mitosis

2000 ◽  
Vol 10 (1) ◽  
pp. 5-8 ◽  
Author(s):  
Philippe Collas ◽  
Jean-Claude Courvalin
Keyword(s):  
Membrane Proteins ◽  
Nuclear Membrane

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

Expression of nuclear membrane proteins in normal, hyperplastic, and neoplastic thyroid epithelial cells

2015 ◽  
Vol 467 (4) ◽  
pp. 427-436 ◽  
Author(s):  
Jieying Wang ◽  
Tetsuo Kondo ◽  
Tetsu Yamane ◽  
Tadao Nakazawa ◽  
Naoki Oish ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Epithelial Cells ◽  
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 Integral Membrane Proteins of the Nuclear Envelope Are Dispersed throughout the Endoplasmic Reticulum during Mitosis

1997 ◽  
Vol 137 (6) ◽  
pp. 1199-1210 ◽  
Author(s):  
Li Yang ◽  
Tinglu Guan ◽  
Larry Gerace
Keyword(s):  
Membrane Proteins ◽  
Nuclear Envelope ◽  
Nuclear Membrane ◽  
Mammalian Cells ◽  
Polyclonal Antibodies ◽  
Integral Membrane Proteins ◽  
Immunogold Electron Microscopy ◽  
Nuclear Pore ◽  
Nuclear Lamins ◽  
Nuclear Membranes

We have analyzed the fate of several integral membrane proteins of the nuclear envelope during mitosis in cultured mammalian cells to determine whether nuclear membrane proteins are present in a vesicle population distinct from bulk ER membranes after mitotic nuclear envelope disassembly or are dispersed throughout the ER. Using immunofluorescence staining and confocal microscopy, we compared the localization of two inner nuclear membrane proteins (laminaassociated polypeptides 1 and 2 [LAP1 and LAP2]) and a nuclear pore membrane protein (gp210) to the distribution of bulk ER membranes, which was determined with lipid dyes (DiOC6 and R6) and polyclonal antibodies. We found that at the resolution of this technique, the three nuclear envelope markers become completely dispersed throughout ER membranes during mitosis. In agreement with these results, we detected LAP1 in most membranes containing ER markers by immunogold electron microscopy of metaphase cells. Together, these findings indicate that nuclear membranes lose their identity as a subcompartment of the ER during mitosis. We found that nuclear lamins begin to reassemble around chromosomes at the end of mitosis at the same time as LAP1 and LAP2 and propose that reassembly of the nuclear envelope at the end of mitosis involves sorting of integral membrane proteins to chromosome surfaces by binding interactions with lamins and chromatin.

scholarly journals Analysis of membrane proteins localizing to the inner nuclear envelope in living cells

2016 ◽  
Vol 215 (4) ◽  
pp. 575-590 ◽  
Author(s):  
Christine J. Smoyer ◽  
Santharam S. Katta ◽  
Jennifer M. Gardner ◽  
Lynn Stoltz ◽  
Scott McCroskey ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Nuclear Membrane ◽  
Fluorescent Protein ◽  
Protein Localization ◽  
Transmembrane Protein ◽  
Protein Composition ◽  
Living Cells ◽  
Correlation Spectroscopy ◽  
Green Fluorescent ◽  
And Function

Understanding the protein composition of the inner nuclear membrane (INM) is fundamental to elucidating its role in normal nuclear function and in disease; however, few tools exist to examine the INM in living cells, and the INM-specific proteome remains poorly characterized. Here, we adapted split green fluorescent protein (split-GFP) to systematically localize known and predicted integral membrane proteins in Saccharomyces cerevisiae to the INM as opposed to the outer nuclear membrane. Our data suggest that components of the endoplasmic reticulum (ER) as well as other organelles are able to access the INM, particularly if they contain a small extraluminal domain. By pairing split-GFP with fluorescence correlation spectroscopy, we compared the composition of complexes at the INM and ER, finding that at least one is unique: Sbh2, but not Sbh1, has access to the INM. Collectively, our work provides a comprehensive analysis of transmembrane protein localization to the INM and paves the way for further research into INM composition and function.

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