A pseudosubstrate peptide inhibits protein kinase C-mediated phosphorylation in permeabilized Rat-1 cells

Thomas Eichholtz; Jacqueline Alblas; Merian van Overveld; Wouter Moolenaar; Hidde Ploegh

doi:10.1016/0014-5793(90)80657-5

A pseudosubstrate peptide inhibits protein kinase C-mediated phosphorylation in permeabilized Rat-1 cells

Thomas Eichholtz, Jacqueline Alblas, Merian van Overveld, Wouter Moolenaar, Hidde Ploegh^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › Academic › peer-review

20 Citations (Scopus)

Abstract

Activation of protein kinase C (PKC) in Rat-1 fibroblasts leads to rapid phosphorylation of an 80-kDa protein, a major substrate of PKC. Digiton-in-permeabilized cells perfectly supported this early response. Introduction of a PKC pseudosubstrate peptide inhibited 80 kDa phosphorylation with an IC₅₀ of 1 μM, while a control peptide had no effect. The results indicate that this semi-intact cell system can be used in combination with the inhibitory pseudosubstrate peptide to study the involvement of PKC in cellular processes.

Original language	English
Pages (from-to)	147-150
Number of pages	4
Journal	FEBS letters
Volume	261
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(90)80657-5
Publication status	Published - 12 Feb 1990

Keywords

(Rat-1 cell)
Protein kinase C
Protein, 80 kDa
Pseudosubstrate peptide
Signal transduction

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10.1016/0014-5793(90)80657-5

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title = "A pseudosubstrate peptide inhibits protein kinase C-mediated phosphorylation in permeabilized Rat-1 cells",

abstract = "Activation of protein kinase C (PKC) in Rat-1 fibroblasts leads to rapid phosphorylation of an 80-kDa protein, a major substrate of PKC. Digiton-in-permeabilized cells perfectly supported this early response. Introduction of a PKC pseudosubstrate peptide inhibited 80 kDa phosphorylation with an IC50 of 1 μM, while a control peptide had no effect. The results indicate that this semi-intact cell system can be used in combination with the inhibitory pseudosubstrate peptide to study the involvement of PKC in cellular processes.",

keywords = "(Rat-1 cell), Protein kinase C, Protein, 80 kDa, Pseudosubstrate peptide, Signal transduction",

author = "Thomas Eichholtz and Jacqueline Alblas and {van Overveld}, Merian and Wouter Moolenaar and Hidde Ploegh",

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AU - Eichholtz, Thomas

AU - Alblas, Jacqueline

AU - van Overveld, Merian

AU - Moolenaar, Wouter

AU - Ploegh, Hidde

PY - 1990/2/12

Y1 - 1990/2/12

N2 - Activation of protein kinase C (PKC) in Rat-1 fibroblasts leads to rapid phosphorylation of an 80-kDa protein, a major substrate of PKC. Digiton-in-permeabilized cells perfectly supported this early response. Introduction of a PKC pseudosubstrate peptide inhibited 80 kDa phosphorylation with an IC50 of 1 μM, while a control peptide had no effect. The results indicate that this semi-intact cell system can be used in combination with the inhibitory pseudosubstrate peptide to study the involvement of PKC in cellular processes.

AB - Activation of protein kinase C (PKC) in Rat-1 fibroblasts leads to rapid phosphorylation of an 80-kDa protein, a major substrate of PKC. Digiton-in-permeabilized cells perfectly supported this early response. Introduction of a PKC pseudosubstrate peptide inhibited 80 kDa phosphorylation with an IC50 of 1 μM, while a control peptide had no effect. The results indicate that this semi-intact cell system can be used in combination with the inhibitory pseudosubstrate peptide to study the involvement of PKC in cellular processes.

KW - (Rat-1 cell)

KW - Protein kinase C

KW - Protein, 80 kDa

KW - Pseudosubstrate peptide

KW - Signal transduction

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AN - SCOPUS:0025189331

SN - 0014-5793

VL - 261

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EP - 150

JO - FEBS letters

JF - FEBS letters

IS - 1

ER -

A pseudosubstrate peptide inhibits protein kinase C-mediated phosphorylation in permeabilized Rat-1 cells

Abstract

Keywords

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