Inner nuclear membrane protein: Difference between revisions
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{{Expert-subject|Molecular and Cellular Biology|date=November 2008}} |
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[[File:Inner_nuclear_membrane_protein_structure,_a_shcematic_representation.jpeg|thumb|right|Inner nuclear membrane proteins structure. Amino-termini (N) and carboxy-termini (C) are indicated in red. Adapted from Holmer and Worman (2001)<ref name=Worman>{{Cite pmid|11766875}}</ref>]] |
[[File:Inner_nuclear_membrane_protein_structure,_a_shcematic_representation.jpeg|thumb|right|Inner nuclear membrane proteins structure. Amino-termini (N) and carboxy-termini (C) are indicated in red. Adapted from Holmer and Worman (2001)<ref name=Worman>{{Cite pmid|11766875}}</ref>]] |
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'''Inner nuclear membrane (INM) proteins''' are [[ |
'''Inner nuclear membrane (INM) proteins''' are [[proteins]] that are [[Integral membrane protein|embedded in]] or associated with the [[inner membrane]] of the [[nuclear envelope]] (NE). There are about 60 INM proteins, most of which are poorly characterized <ref>Iván Méndez-López and Howard J. Worman (2012) Inner nuclear membrane proteins: impact on human disease. Chromosoma Apr;121(2):153-67 [[PubMed_Identifier|PMID]] [http://www.ncbi.nlm.nih.gov/pubmed/22307332 22307332]</ref>. There are very few well characterized INM proteins like lamin B receptor ([[Lamin_B_receptor|LBR]]), the lamina-associated polypeptide-1 (LAP1), the lamina-associated polypeptide-2 (LAP2), [[Emerin|emerin]] and [[LEM_domain-containing_protein_3|MAN1]]. All INM proteins are arranged such that their N-termini facing the nucleoplasm and targeted by various kinases<ref>Georgatos SD (2001) The inner nuclear membrane: simple, or very complex? EMBO J. 20(12):2989-94 [[PubMed_Identifier|PMID]] [http://www.ncbi.nlm.nih.gov/pubmed/11406575 11406575]</ref>. |
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==Structure== |
==Structure== |
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There have been identified several integral nuclear membrane proteins of different size and structure<ref name=Senior>Senior, A and Gerace, L 1988, ’Integral membrane proteins specific to the inner nuclear membrane associated with the nuclear lamina’, The Journal of Cell Biology, vol. 107, no. 6, pp. 2029-2036</ref>. It is proposed that they share some structural features with respect to [[Nucleoplasm|nucleoplasmic]] [[Protein domain|domain(s)]] and lipid soluble domain(s). |
There have been identified several integral nuclear membrane proteins of different size and structure<ref name=Senior>Senior, A and Gerace, L 1988, ’Integral membrane proteins specific to the inner nuclear membrane associated with the nuclear lamina’, The Journal of Cell Biology, vol. 107, no. 6, pp. 2029-2036</ref>. It is proposed that they share some structural features with respect to [[Nucleoplasm|nucleoplasmic]] [[Protein domain|domain(s)]] and lipid soluble domain(s). |
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Revision as of 20:35, 9 April 2012
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Inner nuclear membrane (INM) proteins are proteins that are embedded in or associated with the inner membrane of the nuclear envelope (NE). There are about 60 INM proteins, most of which are poorly characterized [2]. There are very few well characterized INM proteins like lamin B receptor (LBR), the lamina-associated polypeptide-1 (LAP1), the lamina-associated polypeptide-2 (LAP2), emerin and MAN1. All INM proteins are arranged such that their N-termini facing the nucleoplasm and targeted by various kinases[3].
Structure
There have been identified several integral nuclear membrane proteins of different size and structure[4]. It is proposed that they share some structural features with respect to nucleoplasmic domain(s) and lipid soluble domain(s).
Some INM proteins contain common protein domain structures, and can thus be categorised into known protein domain families. These include the LEM-, SUN-, and KASH-domain families. Members of the LEM-domain family play a part in chromatin organisation. SUN- and KASH-domains participate in linking the cytoskeleton and nucleoskeleton through the LINC complex.[5]
Function
Lamins and chromatin found at the nuclear envelope are organised with the assistance of proteins embedded in the INM.[6] INM proteins also aid in organization of nuclear pore complexes (NPCs). The protein mPom121 is targeted to the INM and is necessasry for NPC formation.[4]
Expression
INM proteins are synthesised in one of three places; in the cytoplasm, the cytoplasmic ER, or the outer nuclear membrane (ONM). All require localisation to the INM.[5]
Translation
Since the outer nuclear membrane is continuous with the endoplasmic reticulum it is possible that the inner nuclear membrane proteins are translated on the rough endoplasmic reticulum, whereby the proteins move into the nucleus by lateral diffusion through the nuclear pore[4].
Localization
Current opinion is that INM proteins synthesised in the cytoplasm are transported to the INM through nuclear pore complexes (NPC). [5]
There are several proteins associated with the inner nuclear membrane. It is likely that the majority of them are also associated with the nuclear lamina. Some may interact directly with the nuclear lamina, and some may be associated with it through scaffold proteins [4].
Main categories
Examples of inner nuclear membrane proteins
- Lamin B receptor (LBR)
- Lamina associated polypeptide 1 and 2 (LAP1, LAP2)
- MAN1
- Emerin
- Nurim
Inner nuclear membrane proteins and disease
Mutations in the gene EDM, encoding the INM protein emerin may be the cause of X-linked Emery-Dreifuss muscular dystrophy.[7] As mutations in lamins cause the autosomal dominant form of Emery-Dreifuss muscular dystrophy, and lamins and emerin are known to interact, it has been hypothesised that muscle disease may be caused by a structural defect in the NE brought on by dysfunction in one of these proteins.[1] Tumor cells often show an abherent structure of the nucleus, and is used by pathologists in diagnostics . As changes in the nuclear envelope correspond to functional changes in the nucleus, morphological changes in the nucleus may be involved in carcinogenesis. The regulatory functions of inner nuclear membrane proteins strongly suggest this possibility. [8] Mutations in the gene LBR, encoding lamin B receptor, causes Pelger-Hüet anomaly.[9]
See also
- Nuclear envelope
- Lamin
- Nuclear lamina
- Inner membrane
- Nuclear membrane
- Integral membrane protein
- Transmembrane protein
- Laminopathy
References
- ^ a b Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 11766875, please use {{cite journal}} with
|pmid=11766875instead. - ^ Iván Méndez-López and Howard J. Worman (2012) Inner nuclear membrane proteins: impact on human disease. Chromosoma Apr;121(2):153-67 PMID 22307332
- ^ Georgatos SD (2001) The inner nuclear membrane: simple, or very complex? EMBO J. 20(12):2989-94 PMID 11406575
- ^ a b c d Senior, A and Gerace, L 1988, ’Integral membrane proteins specific to the inner nuclear membrane associated with the nuclear lamina’, The Journal of Cell Biology, vol. 107, no. 6, pp. 2029-2036
- ^ a b c Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 22326668, please use {{cite journal}} with
|pmid=22326668instead. - ^ Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 15688064, please use {{cite journal}} with
|pmid=15688064instead. - ^ Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 22307332, please use {{cite journal}} with
|pmid=22307332instead. - ^ K. Chow, R.E. Factor, K.S. Ullmann (2012) ”The nuclear envelope environment and its cancer connections” Nature Reviews Cancer 12, 196-209 | doi: 10.1038/nrc3219
- ^ Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 12118250, please use {{cite journal}} with
|pmid=12118250instead.
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