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Peptidyl-prolyl isomerase FKBP52 controls chemotropic guidance of neuronal growth cones via regulation of TRPC1 channel opening.

Abstract：

:Immunophilins, including FK506-binding proteins (FKBPs), are protein chaperones with peptidyl-prolyl isomerase (PPIase) activity. Initially identified as pharmacological receptors for immunosuppressants to regulate immune responses via isomerase-independent mechanisms, FKBPs are most highly expressed in the nervous system, where their physiological function as isomerases remains unknown. We demonstrate that FKBP12 and FKBP52 catalyze cis/trans isomerization of regions of TRPC1 implicated in controlling channel opening. FKBP52 mediates stimulus-dependent TRPC1 gating through isomerization, which is required for chemotropic turning of neuronal growth cones to netrin-1 and myelin-associated glycoprotein and for netrin-1/DCC-dependent midline axon guidance of commissural interneurons in the developing spinal cord. By contrast, FKBP12 mediates spontaneous opening of TRPC1 through isomerization and is not required for growth cone responses to netrin-1. Our study demonstrates a novel physiological function of proline isomerases in chemotropic nerve guidance through TRPC1 gating and may have significant implication in clinical applications of immunophilin-related therapeutic drugs.

journal_name

Neuron

journal_title

Neuron

authors

Shim S,Yuan JP,Kim JY,Zeng W,Huang G,Milshteyn A,Kern D,Muallem S,Ming GL,Worley PF

doi

10.1016/j.neuron.2009.09.025

subject

Has Abstract

pub_date

2009-11-25 00:00:00

pages

471-83

issue

4

eissn

0896-6273

issn

1097-4199

pii

S0896-6273(09)00736-3

journal_volume

64

pub_type

杂志文章

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