Abstract
Prolonged activation of protein kinase C (PKC) types α and β by tumor-promoting phorbol esters leads to desensitization of the phorbol ester response, downregulation of protein kinase C activity and depletion of the protein kinase C polypeptide. When the γ isoenzyme of PKC is transiently expressed in COS-1 cells and exposed to phorbol esters, PKC-γ is downregulated in COS cells although these cells do not normally express this subtype. A point mutation in the purative ATP-binding site (Lys-380→Met-380) of the protein kinase C γ isoenzyme which results in a kinase-deficient enzyme does not interfere with this downregulation. Our results suggest that autophosphorylation or constitutive signalling through the protein kinase C-γ kinase domain is not a prerequisite for downregulation of PKC activity.
| Original language | English |
|---|---|
| Pages (from-to) | 262-266 |
| Number of pages | 5 |
| Journal | FEBS Letters |
| Volume | 280 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Mar 25 1991 |
| Externally published | Yes |
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Keywords
- Baculovirus expression
- Downregulation
- Kinase-deficient mutant
- Phorbol ester
- Protein kinase C
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Downregulation of protein kinase C-γ is independent of a functional kinase domain. / Freisewinkel, Ina; Riethmacher, Dieter; Stabel, Silvia.
In: FEBS Letters, Vol. 280, No. 2, 25.03.1991, p. 262-266.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Downregulation of protein kinase C-γ is independent of a functional kinase domain
AU - Freisewinkel, Ina
AU - Riethmacher, Dieter
AU - Stabel, Silvia
PY - 1991/3/25
Y1 - 1991/3/25
N2 - Prolonged activation of protein kinase C (PKC) types α and β by tumor-promoting phorbol esters leads to desensitization of the phorbol ester response, downregulation of protein kinase C activity and depletion of the protein kinase C polypeptide. When the γ isoenzyme of PKC is transiently expressed in COS-1 cells and exposed to phorbol esters, PKC-γ is downregulated in COS cells although these cells do not normally express this subtype. A point mutation in the purative ATP-binding site (Lys-380→Met-380) of the protein kinase C γ isoenzyme which results in a kinase-deficient enzyme does not interfere with this downregulation. Our results suggest that autophosphorylation or constitutive signalling through the protein kinase C-γ kinase domain is not a prerequisite for downregulation of PKC activity.
AB - Prolonged activation of protein kinase C (PKC) types α and β by tumor-promoting phorbol esters leads to desensitization of the phorbol ester response, downregulation of protein kinase C activity and depletion of the protein kinase C polypeptide. When the γ isoenzyme of PKC is transiently expressed in COS-1 cells and exposed to phorbol esters, PKC-γ is downregulated in COS cells although these cells do not normally express this subtype. A point mutation in the purative ATP-binding site (Lys-380→Met-380) of the protein kinase C γ isoenzyme which results in a kinase-deficient enzyme does not interfere with this downregulation. Our results suggest that autophosphorylation or constitutive signalling through the protein kinase C-γ kinase domain is not a prerequisite for downregulation of PKC activity.
KW - Baculovirus expression
KW - Downregulation
KW - Kinase-deficient mutant
KW - Phorbol ester
KW - Protein kinase C
UR - http://www.scopus.com/inward/record.url?scp=0026083348&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0026083348&partnerID=8YFLogxK
U2 - 10.1016/0014-5793(91)80307-O
DO - 10.1016/0014-5793(91)80307-O
M3 - Article
VL - 280
SP - 262
EP - 266
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 2
ER -