ZDHHC5- sinkkisormiproteiini on SARS-viruksen S-proteiinin yksi interaktioproteiini , palmityylitransferaasi 5

https://www.ncbi.nlm.nih.gov/gene/25921

Official Symbol

ZDHHC5

Official Full Name

zinc finger DHHC-type palmitoyltransferase 5

Also known as

DHHC5; ZNF375

Expression

Ubiquitous expression in esophagus (RPKM 30.1), thyroid (RPKM 23.7) and 25 other tissues See more

Preferred Names

palmitoyltransferase ZDHHC5

Names

DHHC-5

membrane-associated DHHC5 zinc finger protein

probable palmitoyltransferase ZDHHC5

zinc finger DHHC domain-containing protein 5

zinc finger DHHC-type containing 5

zinc finger protein 375

zinc finger, DHHC domain containing 5

Related articles in PubMed

1. DHHC5-mediated palmitoylation of S1P receptor subtype 1 determines G-protein coupling. Badawy SMM, et al. Sci Rep, 2017 Nov 29. PMID 29185452, Free PMC Article Abstract
   Sphingosine 1-phosphate (S1P) is a pleiotropic lipid mediator involved in the regulation of immune cell trafficking and vascular permeability acting mainly through G-protein-coupled S1P receptors (S1PRs). However, mechanism underlying how S1PRs are coupled with G-proteins remains unknown. Here we have uncovered that palmitoylation of a prototypical subtype S1P₁R is prerequisite for subsequent inhibitory G-protein (Gi) coupling. We have identified ZDHHC5 as an enzyme for palmitoylation of S1P₁R. Under basal conditions, S1P₁R was functionally associated with DHHC5 in the plasma membranes (PM) and was fully palmitoylated, enabling Gi coupling. Upon stimulation, the receptor underwent internalisation leaving DHHC5 in PM, resulting in depalmitoylation of S1P₁R. We also revealed that while physiological agonist S1P-induced endocytosed S1P₁R readily recycled back to PM, pharmacological FTY720-P-induced endocytosed S1P₁R-positive vesicles became associated with DHHC5 in the later phase, persistently transmitting Gi signals there. This indicates that FTY720-P switches off the S1P signal in PM, while switching on its signal continuously inside the cells. We propose that DHHC5-mediated palmitoylation of S1P₁R determines Gi coupling and its signalling in a spatio/temporal manner.

   PMID:

   29185452

   PMCID:

   PMC5707436

   DOI:

   10.1038/s41598-017-16457-4

2. Systematic siRNA Screen Unmasks NSCLC Growth Dependence by Palmitoyltransferase DHHC5. Tian H, et al. Mol Cancer Res, 2015 Apr. PMID 25573953, Free PMC Article
3. EZH2 Palmitoylation Mediated by ZDHHC5 in p53-Mutant Glioma Drives Malignant Development and Progression. Chen X, et al. Cancer Res, 2017 Sep 15. PMID 28775165
4. Palmitoylation of NOD1 and NOD2 is required for bacterial sensing. Lu Y, et al. Science, 2019 Oct 25. PMID 31649195
5. LXR Activation Down-regulates Lipid Raft Markers FLOT2 and DHHC5 in MCF-7 Breast Cancer Cells. Carbonnelle D, et al. Anticancer Res, 2017 Aug. PMID 28739689

See all (36) citations in PubMed

See citations in PubMed for homologs of this gene provided by HomoloGene

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

1. ZDHHC5-mediated S-palmitoylation is indispensable for NOD1/2 recruitment to bacteria containing phagosomes.
2. DHHC4 and DHHC5 function at different subcellular localizations to control the palmitoylation, plasma membrane localization, and fatty acid uptake activity of the scavenger receptor CD36.
3. High ZDHHC5 expression is associated with Glioma.
4. We demonstrated that LXR stimulation decreases mRNA and protein expression of FLOT2 and DHHC5 in MCF-7 cells. LXR stimulation also reduces Akt phosphorylation and its localization at the plasma membrane
5. Data indicate that DHHC5 has oncogenic capacity and contributes to tumor formation in non-small cell lung cancer.
6. ZDHHC5 and SSTR5 are colocalized at the plasma membrane and coexpression of ZDHHC5 increased palmitoylation of SSTR5 whereas knock-down of endogenous ZDHHC5 by siRNAs decreased it.Many G-protein coupled receptors are palmitoylated in their C-terminal, intracellular regions. So far no enzymes responsible for this modification have been described. We identified an interaction of the membrane proximal helix 8 of somatostatin receptor 5 (SSTR5) with the N-terminal region of the putative palmitoyltransferase ZDHHC5 using the Ras recruitment interaction screening system. ZDHHC5 and SSTR5 are colocalized at the plasma membrane and can be efficiently coimmunoprecipitated from transfected cells. Coexpression of ZDHHC5 in HEK293 cells increased palmitoylation of SSTR5 whereas knock-down of endogenous ZDHHC5 by siRNAs decreased it. Our data identify the first palmitoyltransferase for a G-protein coupled receptor.
7. Data show that palmitoyl acyltransferases DHHC5, DHHC6, and DHHC8 appear to be S-acylated on three cysteine residues within a novel CCX(7-13)C(S/T) motif downstream of a conserved Asp-His-His-Cys cysteine-rich domain.