Abstract
Cytosolic phospholipase A2 (cPLA2) a plays crucial roles in the lipid mediator-biosynthetic pathway following cell activationl. Submicromolar concentrations of Ca2+ are required for cPLA2a to exert its catalytic activity, and this enzyme preferentially hydrolyses phospholipids bearing arachidonic acid2. cPLA2a exists in most mammalian cells, and its activation is regulated by several postreceptor signal transduction events, such as Ca2+ mobilization3, phosphorylation4,5, and gene induction6. Upon Ca2+mobilizing stimulation, cPLA2a translocates rapidly to the perinuclear area7-9. cPLA2a has several functionally distinct regions: an amino-terminal Ca2+-dependent lipid-binding domain (amino acids 18-138) called the C2 domainl0, a carboxy-terminal region (amino acids 179-749) containing the catalytic domain, a putative pleckstrin homology domain 11, and two critical serine residues (Ser505 and Ser727), which undergo activation-directed phosphorylation12. We recently demonstrated that the C2 domain of cPLA2 interacts with vimentin, a major component of intermeiate filaments, in a Ca2+dependent mannerl3. In this report, we have found that another cytoskeletal protein in the cytosol of fibroblasts binds to the C2 domain of cPLA2a.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
M. Murakami, Y. Nakatani, G. Atsumi, K. Inoue, and I. Kudo, Regulatory functions of phospholipase A2, Crit. Rev. Immunol. 17: 225–283 (1997)
J. D. Clark, L.-L. Lin, R. W. Kriz, C. S. Ramesha, L. A. Sultzman, A. Y. Lin, N. Milona, and J. L. Knopf, A novel arachidonic acid-selective cytosolic PLA2 contains a Ca2+-dependent translocation domain with homology to PKC and GAP, Cell, 65: 1043–1051 (1991)
Z. H. Qiu, M. A. Gijon, M. S. Carvalho, D. M. Spencer, and C. C. Leslie, The role of calcium and phosphorylation of cytosolic phospholipase A2 in regulating arachidonic acid release in macrophages, J. Biol. Chem. 273: 8203–8211 (1998)
L.-L. Lin, M. Wartmann, A. Y. Lin, J. L. Knopf, A. Seth, and R. J. Davis, cPLA2 is phosphorylated and activated by MAP kinase, Cell 72: 269–278 (1993)
Y. Nakatani, M. Murakami, I. Kudo, and K. Inoue, Dual regulation of cytosolic phospholipase A2 in mast cells after cross-linking of Fcreceptor, J. Immunol. 153, 796–803 (1994)
L.-L. Lin, A. Y. Lin, and D. L. DeWitt, Interleukin-1 alpha induces the accumulation of cytosolic phospholipase A2 and the release of prostaglandin E2 in human fibroblasts, J. Biol. Chem. 267: 2345–23454 (1992)
S. Glover, T. Bayburt, M. Jonas, E. Chi, and M. H. Gelb, Translocation of the 85-kDa phospholipase A2 from cytosol to the nuclear envelope in rat basophilic leukemia cells stimulated with calcium ionophore or IgE/antigen, J. Biol. Chem. 270: 15359–15367 (1995)
A. R. Schievella, M. K. Regier, W. L. Smith, and L.-L. Lin, Calcium-mediated translocation of cytosolic phospholipase A2 to the nuclear envelope and endoplasmic reticulum, J. Biol. Chem. 270: 30749–30754 (1995)
M. A. Gijon, D. M. Spencer, A. L. Kaiser, and C. C. Leslie, Role of phosphorylation sites and the C2 domain in regulation of cytosolic phospholipase A2, J. Cell Biol. 145: 1219–1232 (1999)
E. A. Nalefski, and J. J. Falke, The C2 domain calcium-binding motif: structural and functional diversity, Protein Sci. 5: 2375–2390 (1996)
M. Mosior, D. A. Six, and E. A. Dennis, Group IV cytosolic phospholipase A2 binds with high affinity and specificity to phosphatidylinositol 4,5-bisphosphate resulting in dramatic increases in activity, J. Biol. Chem. 273: 2184–2191 (1998)
A. G. Borsch-haubold, F. Bartoli, J. Asselin, T. Dudler, R. M. Kramer, R. Apitz-Castro, S. P. Watson, and M. H. Gelb, Identification of the phosphorylation sites of cytosolic phospholipase A2 in agoniststimulated human platelets and HeLa cells, J. Biol. Chem. 273: 4449–4458 (1998)
Y. Nakatani, T. Tanioka, S. Sunaga, M. Murakami, and I. Kudo, Identification of a cellular protein that functionally interacts with the C2 domain of cytosolic phospholipase A2, J. Biol. Chem., 275: 1161–1168 (2000)
S. Inoue, and E. D. Salmon, Force generation by microtubule assembly/disassembly in mitosis and related movements, Mol. Biol. Cell 6: 1619–1640 (1995)
N. Kobayashi, and P. Mundel, A role of microtubules during the formation of cell processes in neuronal and non-neuronal cells, Cell Tissue Res. 291: 163–174 (1998)
C. V. Carman, T. Som, C. M. Kim, and J. L. Benovic, Binding and phosphorylation of tubulin by G protein-coupled receptor kinases, J. Biol. Chem. 273: 20308–20316 (1998)
G. Liao, and G. G. Gundersen, Kinesin is a candidate for cross-bridging microtubules and intermediate filaments, J. Biol. Chem. 273: 9797–9803 (1998)
T. M. Svitkina, A. B. Verkhovsky, and G. G. Borisy, Plectin sidearms mediate interaction of intermediate filaments with microtubules and other components of the cytoskeleton, J. Cell Biol. 135: 991–1007 (1996)
M. L. Shelanski, F. Gaskin, and C. R. Cantor, Microtubule assembly in the absence of added nucleotides, Proc. Natl. Acad. Sci. USA 70: 765–768 (1973)
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2002 Springer Science+Business Media New York
About this chapter
Cite this chapter
Nakatani, Y., Sunaga, S., Murakami, M., Kudo, I. (2002). Cytosolic Phospholipase A2a Interacts With Microtubules. In: Honn, K.V., Marnett, L.J., Nigam, S., Dennis, E., Serhan, C. (eds) Eicosanoids and Other Bioactive Lipids in Cancer, Inflammation, and Radiation Injury, 5. Advances in Experimental Medicine and Biology, vol 507. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-0193-0_4
Download citation
DOI: https://doi.org/10.1007/978-1-4615-0193-0_4
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-4960-0
Online ISBN: 978-1-4615-0193-0
eBook Packages: Springer Book Archive