A new human NHERF1 mutation decreases renal phosphate transporter NPT2a expression by a PTH-independent mechanism.

Autor: Marie Courbebaisse, Christine Leroy, Naziha Bakouh, Christine Salaün, Laurent Beck, Bernard Grandchamp, Gabrielle Planelles, Randy A Hall, Gérard Friedlander, Dominique Prié

Publikováno v: PLoS ONE, Vol 7, Iss 4, p e34764 (2012)

BackgroundThe sodium-hydrogen exchanger regulatory factor 1 (NHERF1) binds to the main renal phosphate transporter NPT2a and to the parathyroid hormone (PTH) receptor. We have recently identified mutations in NHERF1 that decrease renal phosphate reab

Externí odkaz: https://doaj.org/article/0255d0a5a6ce4c6c89a90858da2ad581

Accessory proteins of the zDHHC family of S-acylation enzymes

Autor: Carolina Locatelli, Filip Zmuda, Christine Salaün, Juan Cabrera González, Luke H. Chamberlain

Almost two decades have passed since seminal work in Saccharomyces cerevisiae identified zinc finger DHHC domain-containing (zDHHC) enzymes as S-acyltransferases. These enzymes are ubiquitous in the eukarya domain, with 23 distinct zDHHC-encoding gen

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a95cae3a6afae2b58dedb61c14a048cf
https://strathprints.strath.ac.uk/73926/1/Salaun_etal_JCS_2020_Accessory_proteins_of_the_zDHHC_family_of_S_acylation.pdf

The linker domain of the SNARE protein SNAP25 acts as a flexible molecular spacer that ensures efficient S-acylation

Autor: Luke H. Chamberlain, Christine Salaün, Nicholas C. O. Tomkinson, Jennifer Greaves

Publikováno v: The Journal of Biological Chemistry

S-Acylation of the SNARE protein SNAP25 (synaptosomeassociated protein of 25 kDa) is mediated by a subset of Golgi zinc finger DHHC-type palmitoyltransferase (zDHHC) enzymes, particularly zDHHC17. The ankyrin repeat domain of zDHHC17 interacts with a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97f161043d724a11db1a1ed2dbb7288a
https://strathprints.strath.ac.uk/72170/7/Salaun_etal_JBC_2020_The_linker_domain_of_the_SNARE_protein_SNAP25_acts_as_a_flexible_molecular_spacer.pdf

Substrate selectivity in the zDHHC family of S-acyltransferases

Autor: Marianna Kouskou, Jennifer Greaves, Kimon Lemonidis, Luke H. Chamberlain, Cinta Diez-Ardanuy, Christine Salaün

Publikováno v: Biochemical Society Transactions. 45:751-758

S-acylation is a reversible lipid modification occurring on cysteine residues mediated by a family of membrane-bound ‘zDHHC’ enzymes. S-acylation predominantly results in anchoring of soluble proteins to membrane compartments or in the traffickin

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::494ec25d140726061dde86c069b29a16
https://doi.org/10.1042/bst20160309

Nuclear relocalisation of cytoplasmic poly(A)-binding proteins PABP1 and PABP4 in response to UV irradiation reveals mRNA-dependent export of metazoan PABPs

Autor: Ross C. Anderson, Sheila V. Graham, William A. Richardson, Hannah M. Burgess, Christine Salaün, Nicola K. Gray

Publikováno v: Burgess, H M, Richardson, W A, Anderson, R C, Salaun, C, Graham, S V & Gray, N K 2011, ' Nuclear relocalisation of cytoplasmic poly(A)-binding proteins PABP1 and PABP4 in response to UV irradiation reveals mRNA-dependent export of metazoan PABPs ', Journal of Cell Science, vol. 124, no. 19, pp. 3344-3355 . https://doi.org/10.1242/jcs.087692
Journal of Cell Science

Poly(A)-binding protein 1 (PABP1) has a fundamental role in the regulation of mRNA translation and stability, both of which are crucial for a wide variety of cellular processes. Although generally a diffuse cytoplasmic protein, it can be found in dis

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ff0d0925bb4c87ddab8881ef25e43f6
https://doi.org/10.1242/jcs.087692