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Nuclear pore disassembly from endoplasmic reticulum membranes promotes Ca2+ signalling competency. J Physiol 2008 Jun 15;586(12):2873-88

Date

05/03/2008

Pubmed ID

18450775

Pubmed Central ID

PMC2517208

DOI

10.1113/jphysiol.2008.153379

Scopus ID

2-s2.0-45249108917   15 Citations

Abstract

The functionality of the endoplasmic reticulum (ER) as a Ca(2+) storage organelle is supported by families of Ca(2+) pumps, buffers and channels that regulate Ca(2+) fluxes between the ER lumen and cytosol. Although many studies have identified heterogeneities in Ca(2+) fluxes throughout the ER, the question of how differential functionality of Ca(2+) channels is regulated within proximal regions of the same organelle is unresolved. Here, we studied the in vivo dynamics of an ER subdomain known as annulate lamellae (AL), a cytoplasmic nucleoporin-containing organelle widely used in vitro to study the mechanics of nuclear envelope breakdown. We show that nuclear pore complexes (NPCs) within AL suppress local Ca(2+) signalling activity, an inhibitory influence relieved by heterogeneous dissociation of nucleoporins to yield NPC-denuded ER domains competent at Ca(2+) signalling. Consequently, we propose a novel generalized role for AL - reversible attenuation of resident protein activity - such that regulated AL (dis)assembly via a kinase/phosphatase cycle allows cells to support rapid gain/loss-of-function transitions in cellular physiology.

Author List

Boulware MJ, Marchant JS

Author

Jonathan S. Marchant PhD Chair, Professor in the Cell Biology, Neurobiology and Anatomy department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Animals
Calcium
Calcium Signaling
Cell Membrane
Cells, Cultured
Endoplasmic Reticulum
Nuclear Pore
Oocytes
Xenopus laevis
jenkins-FCD Prod-482 91ad8a360b6da540234915ea01ff80e38bfdb40a