Research ExplorerPublicationsSomatostatin receptor 5 is palmitoylated by the interacting ...

Somatostatin receptor 5 is palmitoylated by the interacting ZDHHC5 palmitoyltransferase.

Standard

Somatostatin receptor 5 is palmitoylated by the interacting ZDHHC5 palmitoyltransferase. / Kokkola, Tarja; Kruse, Claudia; Roy-Pogodzik, Eva-Maria; Pekkinen, Jenna; Bauch, Carola; Hönck, Hans-Hinrich; Hennemann, Hanjo; Kreienkamp, Hans-Jürgen.

In: FEBS LETT, Vol. 585, No. 17, 17, 2011, p. 2665-2670.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Kokkola, T, Kruse, C, Roy-Pogodzik, E-M, Pekkinen, J, Bauch, C, Hönck, H-H, Hennemann, H & Kreienkamp, H-J 2011, 'Somatostatin receptor 5 is palmitoylated by the interacting ZDHHC5 palmitoyltransferase.', FEBS LETT, vol. 585, no. 17, 17, pp. 2665-2670. <http://www.ncbi.nlm.nih.gov/pubmed/21820437?dopt=Citation>

APA

Kokkola, T., Kruse, C., Roy-Pogodzik, E-M., Pekkinen, J., Bauch, C., Hönck, H-H., Hennemann, H., & Kreienkamp, H-J. (2011). Somatostatin receptor 5 is palmitoylated by the interacting ZDHHC5 palmitoyltransferase. FEBS LETT, 585(17), 2665-2670. [17]. http://www.ncbi.nlm.nih.gov/pubmed/21820437?dopt=Citation

Vancouver

Kokkola T, Kruse C, Roy-Pogodzik E-M, Pekkinen J, Bauch C, Hönck H-H et al. Somatostatin receptor 5 is palmitoylated by the interacting ZDHHC5 palmitoyltransferase. FEBS LETT. 2011;585(17):2665-2670. 17.

Bibtex

@article{e1c4ab0b398a4e7fb85a47434d95a813,
title = "Somatostatin receptor 5 is palmitoylated by the interacting ZDHHC5 palmitoyltransferase.",
abstract = "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.",
keywords = "Humans, Microscopy, Fluorescence, Immunoprecipitation, HEK293 Cells, RNA, Small Interfering, Cell Membrane/metabolism, Acyltransferases/genetics/*metabolism, Lipoylation, Receptors, Somatostatin/genetics/*metabolism, Humans, Microscopy, Fluorescence, Immunoprecipitation, HEK293 Cells, RNA, Small Interfering, Cell Membrane/metabolism, Acyltransferases/genetics/*metabolism, Lipoylation, Receptors, Somatostatin/genetics/*metabolism",
author = "Tarja Kokkola and Claudia Kruse and Eva-Maria Roy-Pogodzik and Jenna Pekkinen and Carola Bauch and Hans-Hinrich H{\"o}nck and Hanjo Hennemann and Hans-J{\"u}rgen Kreienkamp",
year = "2011",
language = "English",
volume = "585",
pages = "2665--2670",
journal = "FEBS LETT",
issn = "0014-5793",
publisher = "Elsevier",
number = "17",

}

RIS

TY - JOUR

T1 - Somatostatin receptor 5 is palmitoylated by the interacting ZDHHC5 palmitoyltransferase.

AU - Kokkola, Tarja

AU - Kruse, Claudia

AU - Roy-Pogodzik, Eva-Maria

AU - Pekkinen, Jenna

AU - Bauch, Carola

AU - Hönck, Hans-Hinrich

AU - Hennemann, Hanjo

AU - Kreienkamp, Hans-Jürgen

PY - 2011

Y1 - 2011

N2 - 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.

AB - 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.

KW - Humans

KW - Microscopy, Fluorescence

KW - Immunoprecipitation

KW - HEK293 Cells

KW - RNA, Small Interfering

KW - Cell Membrane/metabolism

KW - Acyltransferases/genetics/metabolism

KW - Lipoylation

KW - Receptors, Somatostatin/genetics/metabolism

KW - Humans

KW - Microscopy, Fluorescence

KW - Immunoprecipitation

KW - HEK293 Cells

KW - RNA, Small Interfering

KW - Cell Membrane/metabolism

KW - Acyltransferases/genetics/metabolism

KW - Lipoylation

KW - Receptors, Somatostatin/genetics/metabolism

M3 - SCORING: Journal article

VL - 585

SP - 2665

EP - 2670

JO - FEBS LETT

JF - FEBS LETT

SN - 0014-5793

IS - 17

M1 - 17

ER -