Getting to know protein kinase D

Johan Van Lint, An Rykx, T. Vántus, Jackie R. Vandenheede

Research output: Contribution to journalArticle

43 Citations (Scopus)

Abstract

The protein kinase D (PKD) enzymes represent a new family of second messenger stimulated kinases, with diacylglycerol as a prime, but not the sole, mediator of activation. Their molecular architecture features a catalytic domain, unrelated to that of all PKC family members, and a large inhibitory, regulatory domain, comprised of two Zinc fingers, and a pleckstrin homology domain. These different sub-domains play distinctive roles in the activation, translocation and biological functions of the kinase. The enzymes have been implicated in signalling mechanisms controlling cell proliferation and programmed cell death and in metastasis, immune responses, and Golgi restructuring and function. A variety of proteins specifically interact with the different sub-domains of the enzymes and direct their wide range of cellular functions.

Original languageEnglish
Pages (from-to)577-581
Number of pages5
JournalInternational Journal of Biochemistry and Cell Biology
Volume34
Issue number6
DOIs
Publication statusPublished - 2002

Fingerprint

4 alpha-glucanotransferase
Diacylglycerol Kinase
Zinc Fingers
Second Messenger Systems
Phosphotransferases
Enzymes
Chemical activation
Catalytic Domain
Cell Death
Diglycerides
Cell Proliferation
Cell proliferation
Cell death
Neoplasm Metastasis
Zinc
Proteins
protein kinase D
Pleckstrin Homology Domains

Keywords

  • Apoptosis
  • Growth factor signalling
  • Protein kinase
  • Second messengers

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology

Cite this

Getting to know protein kinase D. / Lint, Johan Van; Rykx, An; Vántus, T.; Vandenheede, Jackie R.

In: International Journal of Biochemistry and Cell Biology, Vol. 34, No. 6, 2002, p. 577-581.

Research output: Contribution to journalArticle

Lint, Johan Van ; Rykx, An ; Vántus, T. ; Vandenheede, Jackie R. / Getting to know protein kinase D. In: International Journal of Biochemistry and Cell Biology. 2002 ; Vol. 34, No. 6. pp. 577-581.
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