LEM domain-containing protein 3: Difference between revisions
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{{protein | {{Infobox protein | ||
| Name = LEM domain containing protein 3 | | Name = LEM domain containing protein 3 | ||
| caption = | | caption = | ||
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| LocusSupplementaryData = | | LocusSupplementaryData = | ||
}} | }} | ||
It is also associated with [[osteopoikilosis]].<ref name= | '''LEM domain-containing protein 3''' (LEMD3), also known as '''MAN1''', is an integral [[Inner nuclear membrane proteins|protein in the inner nuclear membrane (INM)]] of the [[nuclear envelope]]. It is encoded by the ''LEMD3'' gene<ref name=Worman>{{Cite journal | ||
| last1 = Worman | first1 = H. J. | |||
| last2 = Fong | first2 = L. G. | |||
| last3 = Muchir | first3 = A. | |||
| last4 = Young | first4 = S. G. | |||
| title = Laminopathies and the long strange trip from basic cell biology to therapy | |||
| doi = 10.1172/JCI37679 | |||
| journal = Journal of Clinical Investigation | |||
| volume = 119 | |||
| issue = 7 | |||
| pages = 1825–1836 | |||
| year = 2009 | |||
| pmid = 19587457 | |||
| pmc =2701866 | |||
}}</ref> and was first identified after it was isolated from the [[serum (blood)|serum]] of a patient with a collagen vascular disease.<ref name=PL>{{Cite journal | |||
| last1 = Paulin-Levasseur | first1 = M. | |||
| last2 = Blake | first2 = D. L. | |||
| last3 = Julien | first3 = M. | |||
| last4 = Rouleau | first4 = L. | |||
| title = The MAN antigens are non-lamin constituents of the nuclear lamina in vertebrate cells | |||
| journal = Chromosoma | |||
| volume = 104 | |||
| issue = 5 | |||
| pages = 367–379 | |||
| year = 1996 | |||
| pmid = 8575249 | doi=10.1007/BF00337226 | |||
}}</ref> | |||
==Structure== | |||
The protein is 82.3 kDa and has a 40 amino acid long [[LEM domain|LEM]] [[protein domain|domain]] located at its amino-terminal region. In its carboxyl end it has a [[RNA recognition motif]] (RRM). The LEM domain is also common to two other integral proteins of the INM: [[lamina-associated polypeptide 2]] (LAP2) and [[emerin]].<ref name=Lin>{{Cite journal | |||
| last1 = Lin | first1 = F. | |||
| last2 = Blake | first2 = D. L. | |||
| last3 = Callebaut | first3 = I. | |||
| last4 = Skerjanc | first4 = I. S. | |||
| last5 = Holmer | first5 = L. | |||
| last6 = McBurney | first6 = M. W. | |||
| last7 = Paulin-Levasseur | first7 = M. | |||
| last8 = Worman | first8 = H. J. | |||
| title = MAN1, an inner nuclear membrane protein that shares the LEM domain with lamina-associated polypeptide 2 and emerin | |||
| journal = The Journal of Biological Chemistry | |||
| volume = 275 | |||
| issue = 7 | |||
| pages = 4840–4847 | |||
| year = 2000 | |||
| pmid = 10671519 | doi=10.1074/jbc.275.7.4840 | |||
}}</ref> | |||
The LEM segment enables LEMD3 to attach to the [[barrier-to-autointegration factor]] (BAF), and therefore, indirectly interact with the [[chromatin]]. LEMD3 also has several implications in regulating the [[cytokine]] family such as the [[transforming growth factor beta]] (TGF-β) and [[bone morphogenic protein]] (BMPs). The RRM domain in its carboxylic region attaches to the [[Smads|SMAD (protein)]] proteins, which is involved in mediating TGF-β [[cellular signalling]]. Consequently, LEMD3 indirectly regulates downstream genes. | |||
LEMD3 seems to play an important role in regulating the expression of several fundamental genes. | |||
==LEMD3 and disease== | |||
LEMD3 has been associated with [[laminopathies]]<ref name=Worman /> as well as [[osteopoikilosis]].<ref name=Mumm>{{Cite journal | |||
| last1 = Mumm | first1 = S. | |||
| last2 = Wenkert | first2 = D. | |||
| last3 = Zhang | first3 = X. | |||
| last4 = McAlister | first4 = W. H. | |||
| last5 = Mier | first5 = R. J. | |||
| last6 = Whyte | first6 = M. P. | |||
| doi = 10.1359/jbmr.061102 | |||
| title = Deactivating Germline Mutations in LEMD3 Cause Osteopoikilosis and Buschke-Ollendorff Syndrome, but Not Sporadic Melorheostosis | |||
| journal = Journal of Bone and Mineral Research | |||
| volume = 22 | |||
| issue = 2 | |||
| pages = 243–250 | |||
| year = 2006 | |||
| pmid = 17087626 | |||
| pmc = | |||
}}</ref> Mutations in the ''LEMD3'' gene have been linked to several genetic diseases such as [[osteopoikilosis]], [[melorheostosis]] and [[Buschke-Ollendorff syndrome]]. | |||
==See also== | ==See also== | ||
[[Inner nuclear membrane proteins]] | |||
==References== | ==References== | ||
{{reflist | {{reflist}} | ||
==External links== | ==External links== | ||
* {{MeshName|LEMD3+protein,+human}} | * {{MeshName|LEMD3+protein,+human}} | ||
Revision as of 16:32, 29 June 2016
LEM domain containing protein 3 | |
---|---|
Identifiers | |
Symbol | LEMD3 |
Alt. symbols | MAN1 |
Entrez | 23592 |
HUGO | 28887 |
OMIM | 607844 |
RefSeq | NM_014319 |
UniProt | Q9Y2U8 |
Other data | |
Locus | Chr. 12 q14 |
LEM domain-containing protein 3 (LEMD3), also known as MAN1, is an integral protein in the inner nuclear membrane (INM) of the nuclear envelope. It is encoded by the LEMD3 gene[1] and was first identified after it was isolated from the serum of a patient with a collagen vascular disease.[2]
Structure
The protein is 82.3 kDa and has a 40 amino acid long LEM domain located at its amino-terminal region. In its carboxyl end it has a RNA recognition motif (RRM). The LEM domain is also common to two other integral proteins of the INM: lamina-associated polypeptide 2 (LAP2) and emerin.[3]
The LEM segment enables LEMD3 to attach to the barrier-to-autointegration factor (BAF), and therefore, indirectly interact with the chromatin. LEMD3 also has several implications in regulating the cytokine family such as the transforming growth factor beta (TGF-β) and bone morphogenic protein (BMPs). The RRM domain in its carboxylic region attaches to the SMAD (protein) proteins, which is involved in mediating TGF-β cellular signalling. Consequently, LEMD3 indirectly regulates downstream genes.
LEMD3 seems to play an important role in regulating the expression of several fundamental genes.
LEMD3 and disease
LEMD3 has been associated with laminopathies[1] as well as osteopoikilosis.[4] Mutations in the LEMD3 gene have been linked to several genetic diseases such as osteopoikilosis, melorheostosis and Buschke-Ollendorff syndrome.
See also
Inner nuclear membrane proteins
References
- ↑ 1.0 1.1 Worman, H. J.; Fong, L. G.; Muchir, A.; Young, S. G. (2009). "Laminopathies and the long strange trip from basic cell biology to therapy". Journal of Clinical Investigation. 119 (7): 1825–1836. doi:10.1172/JCI37679. PMC 2701866. PMID 19587457.
- ↑ Paulin-Levasseur, M.; Blake, D. L.; Julien, M.; Rouleau, L. (1996). "The MAN antigens are non-lamin constituents of the nuclear lamina in vertebrate cells". Chromosoma. 104 (5): 367–379. doi:10.1007/BF00337226. PMID 8575249.
- ↑ Lin, F.; Blake, D. L.; Callebaut, I.; Skerjanc, I. S.; Holmer, L.; McBurney, M. W.; Paulin-Levasseur, M.; Worman, H. J. (2000). "MAN1, an inner nuclear membrane protein that shares the LEM domain with lamina-associated polypeptide 2 and emerin". The Journal of Biological Chemistry. 275 (7): 4840–4847. doi:10.1074/jbc.275.7.4840. PMID 10671519.
- ↑ Mumm, S.; Wenkert, D.; Zhang, X.; McAlister, W. H.; Mier, R. J.; Whyte, M. P. (2006). "Deactivating Germline Mutations in LEMD3 Cause Osteopoikilosis and Buschke-Ollendorff Syndrome, but Not Sporadic Melorheostosis". Journal of Bone and Mineral Research. 22 (2): 243–250. doi:10.1359/jbmr.061102. PMID 17087626.
External links
- LEMD3+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)