Atlastin regulates store-operated calcium entry for nerve growth factor-induced neurite outgrowth

Sci Rep. 2017 Feb 27:7:43490. doi: 10.1038/srep43490.

Abstract

Homotypic membrane fusion of the endoplasmic reticulum (ER) is mediated by a class of dynamin-like GTPases known as atlastin (ATL). Depletion of or mutations in ATL cause an unbranched ER morphology and hereditary spastic paraplegia (HSP), a neurodegenerative disease characterized by axon shortening in corticospinal motor neurons and progressive spasticity of the lower limbs. How ER shaping is linked to neuronal defects is poorly understood. Here, we show that dominant-negative mutants of ATL1 in PC-12 cells inhibit nerve growth factor (NGF)-induced neurite outgrowth. Overexpression of wild-type or mutant ATL1 or depletion of ATLs alters ER morphology and affects store-operated calcium entry (SOCE) by decreasing STIM1 puncta formation near the plasma membrane upon calcium depletion of the ER. In addition, blockage of the STIM1-Orai pathway effectively abolishes neurite outgrowth of PC-12 cells stimulated by NGF. These results suggest that SOCE plays an important role in neuronal regeneration, and mutations in ATL1 may cause HSP, partly by undermining SOCE.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Calcium / metabolism*
  • Calcium Signaling / drug effects
  • Cell Line
  • Endoplasmic Reticulum / metabolism
  • Extracellular Space / metabolism
  • GTP-Binding Proteins / genetics
  • GTP-Binding Proteins / metabolism*
  • Gene Expression
  • Humans
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Nerve Growth Factor / metabolism*
  • Nerve Growth Factor / pharmacology
  • Neuronal Outgrowth* / drug effects
  • Neuronal Outgrowth* / genetics
  • Spastic Paraplegia, Hereditary / genetics
  • Spastic Paraplegia, Hereditary / metabolism

Substances

  • Membrane Proteins
  • NGF protein, human
  • Nerve Growth Factor
  • ATL1 protein, human
  • GTP-Binding Proteins
  • Calcium