Endogenous ADP-ribosylation of phosphoprotein B-50/GAP-43 and other neuronal substrates

Advances in Experimental Medicine and Biology

Volumn 419, Issue , 1997, Pages 279-288

  Zwiers, H ^a   Hollenberg, M D ^a   McLean, K N ^a   Philibert, K D ^a  

^a UNIVERSITY OF CALGARY   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; NEUROMODULIN;

ADENOSINE DIPHOSPHATE RIBOSYLATION; BRAIN; CATTLE; CONFERENCE PAPER; NONHUMAN; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; SYNAPTIC MEMBRANE;

BOS TAURUS;

EID: 0030919778     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4419-8632-0_37     Document Type: Conference Paper

References (31)

1. Scaife, R.M., L. Wilson & D.L. Purich. 1991. Microtubule protein ADP-ribosylation in vitro leads to assembly inhibition and rapid depolymerization. Biochem 31: 310-316.
2. Aktories, K., & A. Wegner, 1992. Mechanisms of the cytopathic action of actin-ADP-ribosylating toxins. Mol. Microbiol. 6: 2905-2908.
3. Williamson, K.C. and J. Moss. 1990. Mono-ADP-ribosyltransferases and ADP-ribosylarginine Hydrolases: A mono-ADP-ribosylation Cycle in Animal Cells. In: Moss, J., & M. Vaughan (eds): ADP-ribosylating Toxins and G Proteins: Insights into Signal Transductions. American Society for Microbiology. Washington, D.C., pp. 493-510.
4. Zwiers, H., V.M. Wiegant, P. Schotman & W.H. Gispen. 1978. ACTH-induced inhibition of endogenous rat brain protein phosphorylation in vitro: structure-activity. Neurochem. Res. 3: 455-463.
5. Zwiers, H., P. Schotman & W.H. Gispen. 1980. Purification and some characteristics of an ACTH-sensitive sensitive protein kinase and its substrate protein. J. Neurochem. 34: 1689-1699.
6. Zwiers, H., & P.J. Coggins. 1991. B-50 structure, processing and interaction with ACTH. Progress in Brain Research. 89: 3-16.
7. Skene, J.H.P., & M. Willard. 1981. Changes in Axonally transported proteins during Axon Regeneration in Toad Retinal Ganglion Cells. J. Cell Biology. 89: 86-95.
8. Andreasen, T.J., C.W. Luetje, W. Heideman & D.R. Storm. 1983. Purification of a novel calmodulin binding protein from bovine cerebral cortex membranes. Biochemistry. 22: 4615-4618.
9. Chan, S.Y., K. Murakami & A. Routtenberg. 1986. Phosphoprotein F1: Purification and characterisation of a brain kinase C substrate related to plasticity. J. Neurosci. 6: 3618-3627.
10. Goslin, K., D.J. Schreyer, J.H.P. Skene & G.A. Banker. 1988. Development of neuronal polarity: GAP-43 distinguishes axonal from dendritic growth cones. Nature. 336: 672-674.
11. Gispen, W.H., J.J.M. Leunissen, A.B. Oestreicher, A.J. Verkleij & H. Zwiers. 1985. Presynaptic localization of B-50 phosphoprotein: the ACTH-sensitive protein kinase substrate involved in rat brain phosphoinositide metabolism. Brain Res., 328: 381-385.
12. Strittmatter, S.M., M. Igarashi & M.C. Fishman. 1994. GAP-43 amino terminal peptides modulate growth cone morphology and neurite outgrowth. J. Neurosci. 14: 5503-5513.
13. Strittmatter, S.M., C. Fankhauser, P.C. Huang, H. Mashimo & M.C. Fishman. 1995. Neuronal path-finding is abnormal in mice lacking the neuronal growth cone protein GAP-43. Cell. 80: 445-452.
14. Coggins, P.J., & H. Zwiers. 1991. B-50 (GAP-43): Biochemistry and Functional Neurochemistry of a Neuron-Specific Phosphoprotein. Journal of Neurochemistry. 56: 1095-1106.
15. Alexander, K.A., B.M. Cimler, K.E. Meier, & D.R. Storm. 1987. Regulation of calmodulin binding to P-57. J. Biol. Chem. 262: 6108-6113.
16. 0 is a major growth cone protein subject to regulation by GAP-43. Nature. 344: 836-841.
17. Coggins, P.J., D.D. McIntyre, H.J. Vogel, & H. Zwiers. 1989. Neuronal protein B-50: a proton nuclear-magnetic-resonance study. Biochemical Society Transactions 629th Meeting, London. 17: 785-787.
18. Zhang, M. & H.J. Vogel. Nuclear magnetic resonance studies of the structure of B50/neuromodulin and its interaction with calmodulin. Biochem. Cell Biol. 72: 109-116.
19. Coggins, P.J., K. McLean, A. Nagy & H. Zwiers. 1993. ADP-ribosylation of the neuronal phosphoprotein B-50/GAP-43. J. Neurochem. 60: 368-371.
20. Philbert, K. & H. Zwiers. 1995. Evidence for multi-site ADP-ribosylation of neuronal phosphoprotein B-50/GAP-43. Mol. Cell. Biochem. 149: 183-190.
21. Zwiers, H., & K.D. Philbert. 1996. ADP-ribosylation. In: Neuromethods: Posttranslational Modifications: Techniques and Protocols. Boulton, A.A., G.B. Baker & H. C. Hemmings, Eds. Humana Press Inc: Totowa, N.J. in press.
22. Zwiers, H., K. McLean, K. Philbert & K.A. Sharkey. 1996. A Novel Calmodulin Binding Protein H-20 Related to B-50/GAP43 and BICKS/RC2 is Primarily Located in Nervous Tissue, and is Highly Enriched in Myelin. J. Neurochem. 66: 27th ASN Meeting, Philadelphia, PA. S5A.
23. Coggins, P.J., K. McLean & H. Zwiers. 1993. Neurogranin, a B-50/GAP-43-immunoreactive C-kinase substrate (BICKS), is ADP-ribosylated. FEBS. 335: 109-113.
24. Chao, D., D.L. Severson, H. Zwiers & M.D. Hollenberg. 1995. Radiolabelling of bovine myristoylated alanine-rich protein kinase C substrate (MARCKS) in an ADP-ribosylation reaction. Biochem. Cell Biol. 72: 391-396.
25. Coggins, P.J. & H. Zwiers. 1989. Evidence for a single protein kinase C-mediated phosphorylation site in rat brain protein B-50. J. Neurochem. 53: 1895-1901.
26. Palkiewicz, P., H. Zwiers & F.L. Lorscheider. 1994. ADP-ribosylation of brain neuronal proteins is altered by in vitro and in vivo exposure to inorganic mercury. J. Neurochem. 62: 2049-2052.
27. Skene, J.H.P. & I. Virag. 1989. Posttranslational membrane attachment and dynamic fatty acylation of a neuronal growth cone protein, GAP-43. J. Cell Biol. 108: 613-624.
28. Zuber, M.X., S.M. Strittmatter & M.C. Fishman. 1989. A membrane-targeting signal in the amino terminus of the neuronal protein GAP-43. Nature. 341: 345-348.
29. Milligan, G., M. Parenti & A.I. Magee. 1995. The dynamic role of palmitoylation in signal transduction. TIBS. 20: 181-186.
30. Linder, M.E., C. Kleuss, & S.M. Mumby. 1995. Palmitoylation of G-Protein a Subunits. Methods in Enzymology. 250: 314-329.
31. Saxty, B. A. & S. van Heyningen. 1995. The Purification of a Cysteine-Dependent NAD+ Glycohytlrolase Activity from Bovine Erythrocytes and Evidence that it Exhibits a Novel ADP-ribosyltransferase Activity. Biochem. 310: 931-937.