Resonance assignment of human LARP4A La module.


Journal

Biomolecular NMR assignments
ISSN: 1874-270X
Titre abrégé: Biomol NMR Assign
Pays: Netherlands
ID NLM: 101472371

Informations de publication

Date de publication:
04 2019
Historique:
received: 12 12 2018
accepted: 03 01 2019
pubmed: 12 1 2019
medline: 20 8 2019
entrez: 12 1 2019
Statut: ppublish

Résumé

Human LARP4A belongs to a superfamily of RNA binding proteins called La-related proteins (LARPs). Whilst being a positive regulator of protein synthesis and a promoter of mRNA stability, LARP4A also controls cell morphology and motility in human breast and prostate cancer cells. All LARPs share a characteristic RNA binding unit named the La-module, which despite a high level of primary structure conservation exhibits a great versatility in RNA target selection. Human LARP4A La-module is the most divergent compared with other LARPs and its RNA recognition properties have only recently started to be revealed. Given the key role of LARP4A protein in cancer cell biology, we have initiated a complete NMR characterisation of its La-module and here we report the assignment of

Identifiants

pubmed: 30632004
doi: 10.1007/s12104-019-09871-4
pii: 10.1007/s12104-019-09871-4
pmc: PMC6439165
doi:

Substances chimiques

Autoantigens 0
Ribonucleoproteins 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Pagination

169-172

Subventions

Organisme : Wellcome Trust
ID : 202767/Z/16/Z
Pays : United Kingdom
Organisme : Wellcome Trust
ID : FC001029
Pays : United Kingdom
Organisme : British Heart Foundation
ID : IG/16/2/32273
Pays : United Kingdom
Organisme : Medical Research Council
ID : FC001029
Pays : United Kingdom
Organisme : Cancer Research UK
ID : FC001029
Pays : United Kingdom
Organisme : Wellcome Trust
Pays : United Kingdom

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Auteurs

Isabel Cruz-Gallardo (I)

Randall Centre for Cell and Molecular Biophysics, King's College London, London, SE1 1UL, UK.
Department of Chemistry, King's College London, 7 Trinity Street, London, SE1 1DB, UK.

Luigi Martino (L)

Randall Centre for Cell and Molecular Biophysics, King's College London, London, SE1 1UL, UK.
The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.

Roberta Trotta (R)

Randall Centre for Cell and Molecular Biophysics, King's College London, London, SE1 1UL, UK.
Department of Pharmacy, University of Naples Federico II, Naples, Italy.

Stefano De Tito (S)

Randall Centre for Cell and Molecular Biophysics, King's College London, London, SE1 1UL, UK.
Department of Pharmacy, University of Naples Federico II, Naples, Italy.
Institute of Protein Biochemistry, National Research Council, Via Pietro Castellino 111, 80131, Naples, Italy.

Geoff Kelly (G)

MRC Biomedical NMR Centre, The Francis Crick Institute, London, NW1 1AT, UK.

R Andrew Atkinson (RA)

Randall Centre for Cell and Molecular Biophysics, King's College London, London, SE1 1UL, UK.
Centre for Biomolecular Spectroscopy, King's College London, London, SE1 1UL, UK.

Antonio Randazzo (A)

Department of Pharmacy, University of Naples Federico II, Naples, Italy.

Maria R Conte (MR)

Randall Centre for Cell and Molecular Biophysics, King's College London, London, SE1 1UL, UK. sasi.conte@kcl.ac.uk.
Centre for Biomolecular Spectroscopy, King's College London, London, SE1 1UL, UK. sasi.conte@kcl.ac.uk.

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