Doublecortin kinase-2, a novel doublecortin-related protein kinase associated with terminal segments of axons and dendrites

Arthur M. Edelman, Woo Yang Kim, Dennis Higgins, Elaine G. Goldstein, Michele Oberdoerster, Wade Sigurdson

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

The microtubule (MT)-associated DCX protein plays an essential role in the development of the mammalian cerebral cortex. We report on the identification of a protein kinase, doublecortin kinase-2 (DCK2), with a domain (DC) highly homologous to DCX. DCK2 has MT binding activity associated with its DC domain and protein kinase activity mediated by a kinase domain, organized in a structure in which the two domains are functionally independent. Overexpression of DCK2 stabilizes the MT cytoskeleton against cold-induced depolymerization. Autophosphorylation of DCK2 strongly reduces its affinity for MTs. DCK2 and DCX mRNAs are nervous system-specific and are expressed during the period of cerebrocortical lamination. DCX is down-regulated postnatally, whereas DCK2 persists in abundance into adulthood, suggesting that the DC sequence has previously unrecognized functions in the mature nervous system. In sympathetic neurons, DCK2 is localized to the cell body and to the terminal segments of axons and dendrites. DCK2 may represent a phosphorylation-dependent switch for the reversible control of MT dynamics in the vicinity of neuronal growth cones.

Original languageEnglish (US)
Pages (from-to)8531-8543
Number of pages13
JournalJournal of Biological Chemistry
Volume280
Issue number9
DOIs
StatePublished - Mar 4 2005

Fingerprint

Presynaptic Terminals
Dendrites
Protein Kinases
Phosphotransferases
Microtubules
Neurology
Nervous System
doublecortin protein
Axons
Growth Cones
Depolymerization
Phosphorylation
Microtubule-Associated Proteins
Cytoskeleton
Cerebral Cortex
Neurons
Cones
Cells
Switches
Messenger RNA

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Doublecortin kinase-2, a novel doublecortin-related protein kinase associated with terminal segments of axons and dendrites. / Edelman, Arthur M.; Kim, Woo Yang; Higgins, Dennis; Goldstein, Elaine G.; Oberdoerster, Michele; Sigurdson, Wade.

In: Journal of Biological Chemistry, Vol. 280, No. 9, 04.03.2005, p. 8531-8543.

Research output: Contribution to journalArticle

Edelman, Arthur M. ; Kim, Woo Yang ; Higgins, Dennis ; Goldstein, Elaine G. ; Oberdoerster, Michele ; Sigurdson, Wade. / Doublecortin kinase-2, a novel doublecortin-related protein kinase associated with terminal segments of axons and dendrites. In: Journal of Biological Chemistry. 2005 ; Vol. 280, No. 9. pp. 8531-8543.
@article{779f0c3655474e239cc8ed8ec4e93fb2,
title = "Doublecortin kinase-2, a novel doublecortin-related protein kinase associated with terminal segments of axons and dendrites",
abstract = "The microtubule (MT)-associated DCX protein plays an essential role in the development of the mammalian cerebral cortex. We report on the identification of a protein kinase, doublecortin kinase-2 (DCK2), with a domain (DC) highly homologous to DCX. DCK2 has MT binding activity associated with its DC domain and protein kinase activity mediated by a kinase domain, organized in a structure in which the two domains are functionally independent. Overexpression of DCK2 stabilizes the MT cytoskeleton against cold-induced depolymerization. Autophosphorylation of DCK2 strongly reduces its affinity for MTs. DCK2 and DCX mRNAs are nervous system-specific and are expressed during the period of cerebrocortical lamination. DCX is down-regulated postnatally, whereas DCK2 persists in abundance into adulthood, suggesting that the DC sequence has previously unrecognized functions in the mature nervous system. In sympathetic neurons, DCK2 is localized to the cell body and to the terminal segments of axons and dendrites. DCK2 may represent a phosphorylation-dependent switch for the reversible control of MT dynamics in the vicinity of neuronal growth cones.",
author = "Edelman, {Arthur M.} and Kim, {Woo Yang} and Dennis Higgins and Goldstein, {Elaine G.} and Michele Oberdoerster and Wade Sigurdson",
year = "2005",
month = "3",
day = "4",
doi = "10.1074/jbc.M411027200",
language = "English (US)",
volume = "280",
pages = "8531--8543",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "9",

}

TY - JOUR

T1 - Doublecortin kinase-2, a novel doublecortin-related protein kinase associated with terminal segments of axons and dendrites

AU - Edelman, Arthur M.

AU - Kim, Woo Yang

AU - Higgins, Dennis

AU - Goldstein, Elaine G.

AU - Oberdoerster, Michele

AU - Sigurdson, Wade

PY - 2005/3/4

Y1 - 2005/3/4

N2 - The microtubule (MT)-associated DCX protein plays an essential role in the development of the mammalian cerebral cortex. We report on the identification of a protein kinase, doublecortin kinase-2 (DCK2), with a domain (DC) highly homologous to DCX. DCK2 has MT binding activity associated with its DC domain and protein kinase activity mediated by a kinase domain, organized in a structure in which the two domains are functionally independent. Overexpression of DCK2 stabilizes the MT cytoskeleton against cold-induced depolymerization. Autophosphorylation of DCK2 strongly reduces its affinity for MTs. DCK2 and DCX mRNAs are nervous system-specific and are expressed during the period of cerebrocortical lamination. DCX is down-regulated postnatally, whereas DCK2 persists in abundance into adulthood, suggesting that the DC sequence has previously unrecognized functions in the mature nervous system. In sympathetic neurons, DCK2 is localized to the cell body and to the terminal segments of axons and dendrites. DCK2 may represent a phosphorylation-dependent switch for the reversible control of MT dynamics in the vicinity of neuronal growth cones.

AB - The microtubule (MT)-associated DCX protein plays an essential role in the development of the mammalian cerebral cortex. We report on the identification of a protein kinase, doublecortin kinase-2 (DCK2), with a domain (DC) highly homologous to DCX. DCK2 has MT binding activity associated with its DC domain and protein kinase activity mediated by a kinase domain, organized in a structure in which the two domains are functionally independent. Overexpression of DCK2 stabilizes the MT cytoskeleton against cold-induced depolymerization. Autophosphorylation of DCK2 strongly reduces its affinity for MTs. DCK2 and DCX mRNAs are nervous system-specific and are expressed during the period of cerebrocortical lamination. DCX is down-regulated postnatally, whereas DCK2 persists in abundance into adulthood, suggesting that the DC sequence has previously unrecognized functions in the mature nervous system. In sympathetic neurons, DCK2 is localized to the cell body and to the terminal segments of axons and dendrites. DCK2 may represent a phosphorylation-dependent switch for the reversible control of MT dynamics in the vicinity of neuronal growth cones.

UR - http://www.scopus.com/inward/record.url?scp=14844323616&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=14844323616&partnerID=8YFLogxK

U2 - 10.1074/jbc.M411027200

DO - 10.1074/jbc.M411027200

M3 - Article

C2 - 15611072

AN - SCOPUS:14844323616

VL - 280

SP - 8531

EP - 8543

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 9

ER -