Skip to main content
NCBI home page
Plant Physiology logoLink to Plant Physiology
. 1992 Dec;100(4):2116–2120. doi: 10.1104/pp.100.4.2116

Association of Phosphatidylinositol Kinase, Phosphatidylinositol Monophosphate Kinase, and Diacylglycerol Kinase with the Cytoskeleton and F-Actin Fractions of Carrot (Daucus carota L.) Cells Grown in Suspension Culture 1

Response to Cell Wall-Degrading Enzymes

Zheng Tan 1, Wendy F Boss 1
PMCID: PMC1075917  PMID: 16653250

Abstract

Phosphatidylinositol kinase (PI), phosphatidylinositol monophosphate (PIP) kinase, and diacylglycerol (DAG) kinase activities were detected in the cytoskeletal fraction isolated from microsomes and plasma membranes of carrot (Daucus carota L.) cells grown in suspension culture. The lipid kinase activities were associated with the actin filament fraction (F-actin fraction) isolated from the cytoskeleton. The PI and PIP kinase activity in the F-actin fraction significantly increased after cells were treated with Driselase, a mixture of cell wall-degrading enzymes; however, the DAG kinase activity in the F-actin fraction was unaffected by the Driselase treatment. These data indicate that at least one form of PI, PIP, and DAG kinase preferentially associates with actin filaments and/or actin binding proteins and that cytoskeletal-associated PI and PIP kinase activities can change in response to external stimulation.

Full text

PDF
2116

Images in this article

2118Figure 2
on p.2118

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Berridge M. J. Inositol trisphosphate and diacylglycerol: two interacting second messengers. Annu Rev Biochem. 1987;56:159–193. doi: 10.1146/annurev.bi.56.070187.001111. [DOI] [PubMed] [Google Scholar]
  2. Boss W. F., Ruesink A. W. Isolation and Characterization of Concanavalin A-labeled Plasma Membranes of Carrot Protoplasts. Plant Physiol. 1979 Dec;64(6):1005–1011. doi: 10.1104/pp.64.6.1005. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Carpenter C. L., Cantley L. C. Phosphoinositide kinases. Biochemistry. 1990 Dec 25;29(51):11147–11156. doi: 10.1021/bi00503a001. [DOI] [PubMed] [Google Scholar]
  4. Chen Q., Boss W. F. Short-term treatment with cell wall degrading enzymes increases the activity of the inositol phospholipid kinases and the vanadate-sensitive ATPase of carrot cells. Plant Physiol. 1990 Dec;94(4):1820–1829. doi: 10.1104/pp.94.4.1820. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Chen Q., Brglez I., Boss W. F. Inositol phospholipids as plant second messengers. Symp Soc Exp Biol. 1991;45:159–175. [PubMed] [Google Scholar]
  6. Demma M., Warren V., Hock R., Dharmawardhane S., Condeelis J. Isolation of an abundant 50,000-dalton actin filament bundling protein from Dictyostelium amoebae. J Biol Chem. 1990 Feb 5;265(4):2286–2291. [PubMed] [Google Scholar]
  7. Einspahr K. J., Thompson G. A. Transmembrane Signaling via Phosphatidylinositol 4,5-Bisphosphate Hydrolysis in Plants. Plant Physiol. 1990 Jun;93(2):361–366. doi: 10.1104/pp.93.2.361. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Gallagher S. R., Leonard R. T. Effect of vanadate, molybdate, and azide on membrane-associated ATPase and soluble phosphatase activities of corn roots. Plant Physiol. 1982 Nov;70(5):1335–1340. doi: 10.1104/pp.70.5.1335. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Gross W., Yang W., Boss W. F. Release of carrot plasma membrane-associated phosphatidylinositol kinase by phospholipase A2 and activation by a 70 kDa protein. Biochim Biophys Acta. 1992 Feb 19;1134(1):73–80. doi: 10.1016/0167-4889(92)90029-b. [DOI] [PubMed] [Google Scholar]
  10. Haus U., Hartmann H., Trommler P., Noegel A. A., Schleicher M. F-actin capping by cap32/34 requires heterodimeric conformation and can be inhibited with PIP2. Biochem Biophys Res Commun. 1991 Dec 16;181(2):833–839. doi: 10.1016/0006-291x(91)91265-e. [DOI] [PubMed] [Google Scholar]
  11. Janmey P. A., Stossel T. P. Modulation of gelsolin function by phosphatidylinositol 4,5-bisphosphate. Nature. 1987 Jan 22;325(6102):362–364. doi: 10.1038/325362a0. [DOI] [PubMed] [Google Scholar]
  12. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  13. Lassing I., Lindberg U. Specificity of the interaction between phosphatidylinositol 4,5-bisphosphate and the profilin:actin complex. J Cell Biochem. 1988 Jul;37(3):255–267. doi: 10.1002/jcb.240370302. [DOI] [PubMed] [Google Scholar]
  14. Majerus P. W., Connolly T. M., Deckmyn H., Ross T. S., Bross T. E., Ishii H., Bansal V. S., Wilson D. B. The metabolism of phosphoinositide-derived messenger molecules. Science. 1986 Dec 19;234(4783):1519–1526. doi: 10.1126/science.3024320. [DOI] [PubMed] [Google Scholar]
  15. Mescher M. F., Jose M. J., Balk S. P. Actin-containing matrix associated with the plasma membrane of murine tumour and lymphoid cells. Nature. 1981 Jan 15;289(5794):139–144. doi: 10.1038/289139a0. [DOI] [PubMed] [Google Scholar]
  16. Payrastre B., van Bergen en Henegouwen P. M., Breton M., den Hartigh J. C., Plantavid M., Verkleij A. J., Boonstra J. Phosphoinositide kinase, diacylglycerol kinase, and phospholipase C activities associated to the cytoskeleton: effect of epidermal growth factor. J Cell Biol. 1991 Oct;115(1):121–128. doi: 10.1083/jcb.115.1.121. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Smith P. K., Krohn R. I., Hermanson G. T., Mallia A. K., Gartner F. H., Provenzano M. D., Fujimoto E. K., Goeke N. M., Olson B. J., Klenk D. C. Measurement of protein using bicinchoninic acid. Anal Biochem. 1985 Oct;150(1):76–85. doi: 10.1016/0003-2697(85)90442-7. [DOI] [PubMed] [Google Scholar]
  18. Vandekerckhove J. Actin-binding proteins. Curr Opin Cell Biol. 1990 Feb;2(1):41–50. doi: 10.1016/s0955-0674(05)80029-8. [DOI] [PubMed] [Google Scholar]
  19. Xu P., Lloyd C. W., Staiger C. J., Drobak B. K. Association of Phosphatidylinositol 4-Kinase with the Plant Cytoskeleton. Plant Cell. 1992 Aug;4(8):941–951. doi: 10.1105/tpc.4.8.941. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Yin H. L., Iida K., Janmey P. A. Identification of a polyphosphoinositide-modulated domain in gelsolin which binds to the sides of actin filaments. J Cell Biol. 1988 Mar;106(3):805–812. doi: 10.1083/jcb.106.3.805. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Yonezawa N., Nishida E., Iida K., Yahara I., Sakai H. Inhibition of the interactions of cofilin, destrin, and deoxyribonuclease I with actin by phosphoinositides. J Biol Chem. 1990 May 25;265(15):8382–8386. [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES