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

MALTER, JAMES S.

JOURNAL OF NEUROCHEMISTRY

WILEY-BLACKWELL PUBLISHING, INC

Año: 2016 vol. 137 p. 744 - 744

0022-3042

xonal growth cone motility requires precise regulation ofadhesion to navigate the complex environment of the nervoussystem and reach its target. Myristoylated alanine-rich Ckinase substrate (MARCKS) protein is enriched in the developingbrain and plays an important, phosphorylation-dependentrole in the modulation of axonal growth cone adhesion.The ratio of phospho-MARCKS (MARCKS-P) to totalMARCKS controls adhesion modulation and spreading of theaxonal 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) isalso expressed in the developing brain. Here, we show thatPin1 is present in the growth cone, interacts with MARCKS-P,and regulates its dephosphorylation. We also describedmorphological alterations in the corpus callosum and cerebralcortex fibers of the Pin1 knockout mouse brain that may becaused by the misregulation of MARCKS-P and alterations ofneuronal adhesion