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c-Jun N-terminal kinase-3 (JNK3)/stress-activated protein kinase-beta (SAPKbeta) binds and phosphorylates the neuronal microtubule regulator SCG10.
Journal article

c-Jun N-terminal kinase-3 (JNK3)/stress-activated protein kinase-beta (SAPKbeta) binds and phosphorylates the neuronal microtubule regulator SCG10.

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  • 2001-11-24
Published in:
  • FEBS letters. - 2001
Amino Acid Sequence
Amino Acids
Animals
Blotting, Western
COS Cells
Calcium-Binding Proteins
Carrier Proteins
Growth Cones
Intracellular Signaling Peptides and Proteins
MAP Kinase Signaling System
Mass Spectrometry
Membrane Proteins
Mice
Microtubule Proteins
Mitogen-Activated Protein Kinase 10
Mitogen-Activated Protein Kinase Kinases
Mitogen-Activated Protein Kinases
Molecular Sequence Data
Nerve Growth Factors
Phosphorylation
Protein Binding
Protein-Tyrosine Kinases
Rats
Rats, Sprague-Dawley
Substrate Specificity
p38 Mitogen-Activated Protein Kinases
English The neuronal growth-associated protein SCG10 is enriched in the growth cones of neurons where it destabilizes microtubules and thus contributes to the dynamic assembly and disassembly of microtubules. Since its microtubule-destabilizing activity is regulated by phosphorylation, SCG10 may link extracellular signals to rearrangements of the neuronal cytoskeleton. To identify signal transduction pathways that may lead to SCG10 phosphorylation, we tested a series of serine-threonine-directed protein kinases that phosphorylate SCG10 in vitro. We demonstrate that purified SCG10 can be phosphorylated by two subclasses of mitogen-activated protein (MAP) kinases, c-Jun N-terminal/stress-activated protein kinase (JNK/SAPK) and p38 MAP kinase. Moreover, SCG10 was found to bind tightly and specifically to JNK3/SAPKbeta. JNK3/SAPKbeta phosphorylation occurs at Ser-62 and Ser-73, residues that result in reduced microtubule-destabilizing activity for SCG10. Endogenous SCG10 also undergoes increased phosphorylation in sympathetic neurons at times of JNK3/SAPKbeta activation following deprivation from nerve growth factor. Together these observations indicate that activation of JNK/SAPKs provides a pathway for phosphorylation of SCG10 and control of growth cone microtubule formation following neuronal exposure to cellular stresses.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://sonar.ch/global/documents/189585
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