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French painter and exponent of fauvism (1876-1958) (同)Maurice de Vlaminck

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/02/27 19:22:45」(JST)

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Nuclear lamins, also known as Class V intermediate filaments, are fibrous proteins providing structural function and transcriptional regulation in the cell nucleus. Nuclear lamins interact with membrane-associated proteins to form the nuclear lamina on the interior of the nuclear envelope. They are involved in the breakdown and reformation of the nuclear envelope during mitosis, as well as the positioning of nuclear pores.

A, B, and C types

In animal cells, there are A- and B-type lamins, which differ in their length and pI. Human cells have three differentially regulated genes.

B-type lamins are present in every cell. B type lamins, B1 and B2, are expressed from the LMNB1 and LMNB2 genes on 5q23 and 19q13, respectively.
A-type lamins are expressed only following gastrulation. Lamin A and C are the most common A-type lamins and are splice variants of the LMNA gene found at 1q21.
C-type lamins are also subject to tissue-specific expression.

Function and structure

These proteins localize to two regions of the nuclear compartment, the nuclear lamina -- a proteinaceous structure layer subjacent to the inner surface of the nuclear envelope and throughout the nucleoplasm in the nucleoplasmic "veil".

Comparison of the lamins to cytoskeletal intermediate filaments shows that lamins have an extra 42 residues (six heptads) within coil 1b. The c-terminal tail domain contains a nuclear localization signal (NLS), an Ig-fold-like domain, and in most cases a carboxy-terminal CaaX box that is isoprenylated and carboxymethylated (lamin C does not have a CAAX box). Lamin A is further processed to remove the last 15 amino acids and its farnesylated cysteine.

Lamin A and lamin C form homodimers which associate head to tail.

During mitosis, lamins are phosphorylated by Mitosis-Promoting Factor (MPF), which drives the disassembly of the lamina and the nuclear envelope. After chromosome segregation, dephosphorylation of nuclear lamins promotes reassembly of the nuclear envelope.

External links

Lamins at the US National Library of Medicine Medical Subject Headings (MeSH)

UpToDate Contents

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English Journal

In silico investigation of molecular mechanism of laminopathy caused by a point mutation (R482W) in lamin A/C protein.

Rajendran V, Purohit R, Sethumadhavan R.SourceBioinformatics Division, School of Bio Sciences and Technology, Vellore Institute of Technology University, Vellore, 632014, Tamil Nadu, India.
Amino acids.Amino Acids.2012 Aug;43(2):603-15. Epub 2011 Oct 12.
Lamin A/C proteins are the major components of a thin proteinaceous filamentous meshwork, the lamina, that underlies the inner nuclear membrane. A few specific mutations in the lamin A/C gene cause a disease with remarkably different clinical features: FPLD, or familial partial lipodystrophy (Dunnig
PMID 21989830

Japanese Journal

第三回千葉医学会奨励賞プロテオミクスの手法によるラミンAの機能解析 : 早老症であるHutchinson-Gilford Progeria Syndromeにおける動脈硬化性疾患の原因解明に向けて

木下大輔
千葉医学雑誌 88(1), 47-51, 2012-02
老化や死は,生物にとって避けることのできないものであり,長年に亘って老化に関する研究や議論が続けられている。早老症は,若い頃から老化の生理学的特徴を示すものであり,Hutchinson-Gilford progeria syndrome(HGPS)が促進的な老化過程と類似していることから,同疾患は老化研究のモデルとして注目を浴びている[1]。 HGPSは平均寿命13歳,主な死因は心筋梗塞等の動脈硬 …
NAID 40019203810

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★リンクテーブル★

リンク元	「ラミン」
拡張検索	「ethyldimethylaminopropyl carbodiimide」「monoethanolamine oleate」「cobalt 57-cyanocobalamin」「lamina basalis」