Protein interacting with NIMA (never in mitosis A)-1 regulates axonal growth cone adhesion and spreading through myristoylated alanine-rich C kinase substrate isomerization

Lucas J. Sosa, James S. Malter, Jie Hu, Florentyna Bustos Plonka, Mariana Oksdath, Alvaro F. Nieto Guil, Santiago Quiroga, Karl H. Pfenninger

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Axonal growth cone motility requires precise regulation of adhesion to navigate the complex environment of the nervous system and reach its target. Myristoylated alanine-rich C kinase substrate (MARCKS) protein is enriched in the developing brain and plays an important, phosphorylation-dependent role in the modulation of axonal growth cone adhesion. The ratio of phospho-MARCKS (MARCKS-P) to total MARCKS controls adhesion modulation and spreading of the axonal growth cone. Pin1, a peptidyl-prolyl cis/trans isomerase (PPIase) that recognizes and binds to phosphorylated serine/threonine residues preceded by a proline (pSer/Thr-Pro) is also expressed in the developing brain. Here, we show that Pin1 is present in the growth cone, interacts with MARCKS-P, and regulates its dephosphorylation. We also described morphological alterations in the corpus callosum and cerebral cortex fibers of the Pin1 knockout mouse brain that may be caused by the misregulation of MARCKS-P and alterations of neuronal adhesion.

Original languageEnglish (US)
JournalJournal of Neurochemistry
DOIs
StateAccepted/In press - 2016

Fingerprint

Growth Cones
Isomerization
Mitosis
Cones
Adhesion
Brain
Proteins
Modulation
Peptidylprolyl Isomerase
Phosphorylation
Corpus Callosum
Neurology
Threonine
Proline
Knockout Mice
Cerebral Cortex
Serine
Nervous System
myristoylated alanine-rich C kinase substrate
Fibers

Keywords

  • MARCKS
  • Brain development
  • Corpus callosum
  • Growth cone adhesion
  • Isomerization
  • Pin1

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

Cite this

Protein interacting with NIMA (never in mitosis A)-1 regulates axonal growth cone adhesion and spreading through myristoylated alanine-rich C kinase substrate isomerization. / Sosa, Lucas J.; Malter, James S.; Hu, Jie; Bustos Plonka, Florentyna; Oksdath, Mariana; Nieto Guil, Alvaro F.; Quiroga, Santiago; Pfenninger, Karl H.

In: Journal of Neurochemistry, 2016.

Research output: Contribution to journalArticle

Sosa, Lucas J. ; Malter, James S. ; Hu, Jie ; Bustos Plonka, Florentyna ; Oksdath, Mariana ; Nieto Guil, Alvaro F. ; Quiroga, Santiago ; Pfenninger, Karl H. / Protein interacting with NIMA (never in mitosis A)-1 regulates axonal growth cone adhesion and spreading through myristoylated alanine-rich C kinase substrate isomerization. In: Journal of Neurochemistry. 2016.
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AU - Sosa, Lucas J.

AU - Malter, James S.

AU - Hu, Jie

AU - Bustos Plonka, Florentyna

AU - Oksdath, Mariana

AU - Nieto Guil, Alvaro F.

AU - Quiroga, Santiago

AU - Pfenninger, Karl H.

PY - 2016

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N2 - Axonal growth cone motility requires precise regulation of adhesion to navigate the complex environment of the nervous system and reach its target. Myristoylated alanine-rich C kinase substrate (MARCKS) protein is enriched in the developing brain and plays an important, phosphorylation-dependent role in the modulation of axonal growth cone adhesion. The ratio of phospho-MARCKS (MARCKS-P) to total MARCKS controls adhesion modulation and spreading of the axonal growth cone. Pin1, a peptidyl-prolyl cis/trans isomerase (PPIase) that recognizes and binds to phosphorylated serine/threonine residues preceded by a proline (pSer/Thr-Pro) is also expressed in the developing brain. Here, we show that Pin1 is present in the growth cone, interacts with MARCKS-P, and regulates its dephosphorylation. We also described morphological alterations in the corpus callosum and cerebral cortex fibers of the Pin1 knockout mouse brain that may be caused by the misregulation of MARCKS-P and alterations of neuronal adhesion.

AB - Axonal growth cone motility requires precise regulation of adhesion to navigate the complex environment of the nervous system and reach its target. Myristoylated alanine-rich C kinase substrate (MARCKS) protein is enriched in the developing brain and plays an important, phosphorylation-dependent role in the modulation of axonal growth cone adhesion. The ratio of phospho-MARCKS (MARCKS-P) to total MARCKS controls adhesion modulation and spreading of the axonal growth cone. Pin1, a peptidyl-prolyl cis/trans isomerase (PPIase) that recognizes and binds to phosphorylated serine/threonine residues preceded by a proline (pSer/Thr-Pro) is also expressed in the developing brain. Here, we show that Pin1 is present in the growth cone, interacts with MARCKS-P, and regulates its dephosphorylation. We also described morphological alterations in the corpus callosum and cerebral cortex fibers of the Pin1 knockout mouse brain that may be caused by the misregulation of MARCKS-P and alterations of neuronal adhesion.

KW - MARCKS

KW - Brain development

KW - Corpus callosum

KW - Growth cone adhesion

KW - Isomerization

KW - Pin1

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