Picture of wind turbine against blue sky

Open Access research with a real impact...

The Strathprints institutional repository is a digital archive of University of Strathclyde research outputs.

The Energy Systems Research Unit (ESRU) within Strathclyde's Department of Mechanical and Aerospace Engineering is producing Open Access research that can help society deploy and optimise renewable energy systems, such as wind turbine technology.

Explore wind turbine research in Strathprints

Explore all of Strathclyde's Open Access research content

Endoplasmic reticulum localization of DHHC palmitoyltransferases mediated by lysine-based sorting signals

Gorleku, Oforiwa A and Barns, Anna-Marie and Prescott, Gerald R and Greaves, Jennifer and Chamberlain, Luke H (2011) Endoplasmic reticulum localization of DHHC palmitoyltransferases mediated by lysine-based sorting signals. Journal of Biological Chemistry, 286. pp. 39573-39584.

Full text not available in this repository. (Request a copy from the Strathclyde author)


Intracellular palmitoylation dynamics are regulated by a family of 24 DHHC palmitoyl transferases, which are localized in a compartment-specific manner. The majority of DHHC proteins localize to endoplasmic reticulum (ER) and Golgi membranes, and a small number target to post-Golgi membranes. To-date, there are no reports of the fine mapping of sorting signals in mammalian DHHC proteins, and thus it is unclear how spatial distribution of the DHHC family is achieved. Here, we have identified and characterized lysine-based sorting signals that determine the restricted localization of DHHC4 and DHHC6 to ER membranes. The ER targeting signal in DHHC6 conforms to a KKxx motif, whereas the signal in DHHC4 is a distinct Kxx motif. The identified dilysine signals are sufficient to specify ER localization as adding the C-terminal pentapeptide sequences from DHHC4 or DHHC6, which contain these Kxx and KKxx motifs, to the C-terminus of DHHC3 redistributes this palmitoyl transferase from Golgi to ER membranes. Recent work proposed that palmitoylation of newly-synthesized peripheral membrane proteins occurs predominantly at the Golgi. Indeed, previous analyses of the peripheral membrane proteins, SNAP25 and cysteine-string protein is fully consistent with their initial palmitoylation being mediated by Golgi-localized DHHC proteins. Interestingly, ER-localized DHHC3 is able to palmitoylate SNAP25 and cysteine-string protein to a similar level as wild-type Golgi-localized DHHC3 in co-expression studies. These results suggest that targeting of intrinsically active DHHC proteins to defined membrane compartments is an important factor contributing to spatially-restricted patterns of substrate palmitoylation. compartments.