Literature DB >> 17451680

Proteins that associate with lamins: many faces, many functions.

Eric C Schirmer1, Roland Foisner.   

Abstract

Lamin-associated polypeptides (LAPs) comprise inner nuclear membrane proteins tightly associated with the peripheral lamin scaffold as well as proteins forming stable complexes with lamins in the nucleoplasm. The involvement of LAPs in a wide range of human diseases may be linked to an equally bewildering range of their functions, including sterol reduction, histone modification, transcriptional repression, and Smad- and beta-catenin signaling. Many LAPs are likely to be at the center of large multi-protein complexes, components of which may dictate their functions, and a few LAPs have defined enzymatic activities. Here we discuss the definition of LAPs, review their many binding partners, elaborate their functions in nuclear architecture, chromatin organization, gene expression and signaling, and describe what is currently known about their links to human disease.

Entities:  

Mesh:

Substances:

Year:  2007        PMID: 17451680     DOI: 10.1016/j.yexcr.2007.03.012

Source DB:  PubMed          Journal:  Exp Cell Res        ISSN: 0014-4827            Impact factor:   3.905


  73 in total

1.  Structure and stability of the lamin A tail domain and HGPS mutant.

Authors:  Zhao Qin; Agnieszka Kalinowski; Kris Noel Dahl; Markus J Buehler
Journal:  J Struct Biol       Date:  2011-05-24       Impact factor: 2.867

Review 2.  Many mechanisms, one entrance: membrane protein translocation into the nucleus.

Authors:  Nikolaj Zuleger; Alastair R W Kerr; Eric C Schirmer
Journal:  Cell Mol Life Sci       Date:  2012-02-12       Impact factor: 9.261

Review 3.  The nuclear envelope as a chromatin organizer.

Authors:  Nikolaj Zuleger; Michael I Robson; Eric C Schirmer
Journal:  Nucleus       Date:  2011-09-01       Impact factor: 4.197

Review 4.  Lamin-binding Proteins.

Authors:  Katherine L Wilson; Roland Foisner
Journal:  Cold Spring Harb Perspect Biol       Date:  2010-02-17       Impact factor: 10.005

Review 5.  The nuclear envelope.

Authors:  Martin W Hetzer
Journal:  Cold Spring Harb Perspect Biol       Date:  2010-03       Impact factor: 10.005

6.  Inheriting nuclear organization: can nuclear lamins impart spatial memory during post-mitotic nuclear assembly?

Authors:  Catherine Martin; Songbi Chen; Dean A Jackson
Journal:  Chromosome Res       Date:  2010-06-22       Impact factor: 5.239

7.  Regulation of prelamin A but not lamin C by miR-9, a brain-specific microRNA.

Authors:  Hea-Jin Jung; Catherine Coffinier; Youngshik Choe; Anne P Beigneux; Brandon S J Davies; Shao H Yang; Richard H Barnes; Janet Hong; Tao Sun; Samuel J Pleasure; Stephen G Young; Loren G Fong
Journal:  Proc Natl Acad Sci U S A       Date:  2012-01-30       Impact factor: 11.205

Review 8.  Nuclear shape, mechanics, and mechanotransduction.

Authors:  Kris Noel Dahl; Alexandre J S Ribeiro; Jan Lammerding
Journal:  Circ Res       Date:  2008-06-06       Impact factor: 17.367

9.  Analysis of prelamin A biogenesis reveals the nucleus to be a CaaX processing compartment.

Authors:  Jemima Barrowman; Corinne Hamblet; Carolyn M George; Susan Michaelis
Journal:  Mol Biol Cell       Date:  2008-10-15       Impact factor: 4.138

10.  Skin deep: what can the study of dermal fibroblasts teach us about dilated cardiomyopathy?

Authors:  Brian C Jensen
Journal:  J Mol Cell Cardiol       Date:  2009-12-11       Impact factor: 5.000

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.