Nuclear pore disassembly from endoplasmic reticulum membranes promotes Ca2+ signalling competency. J Physiol 2008 Jun 15;586(12):2873-88
Date
05/03/2008Pubmed ID
18450775Pubmed Central ID
PMC2517208DOI
10.1113/jphysiol.2008.153379Scopus ID
2-s2.0-45249108917 (requires institutional sign-in at Scopus site) 18 CitationsAbstract
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 JSAuthor
Jonathan S. Marchant PhD Chair, Professor in the Cell Biology, Neurobiology and Anatomy department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
AnimalsCalcium
Calcium Signaling
Cell Membrane
Cells, Cultured
Endoplasmic Reticulum
Nuclear Pore
Oocytes
Xenopus laevis
