The coordinating role of IQGAP1 in the regulation of local, endosome-specific actin networks.

Autor:	Samson EB; Department of Bioengineering, Rice University, Houston, TX 77030, USA., Tsao DS; Department of Bioengineering, Rice University, Houston, TX 77030, USA., Zimak J; Department of Bioengineering, Rice University, Houston, TX 77030, USA., McLaughlin RT; Graduate Program in Systems, Synthetic and Physical Biology, Rice University, Houston, TX 77030, USA., Trenton NJ; Department of Bioengineering, Rice University, Houston, TX 77030, USA., Mace EM; Center for Human Immunobiology, Baylor College of Medicine and Texas Children's Hospital, Houston, TX 77030, USA., Orange JS; Center for Human Immunobiology, Baylor College of Medicine and Texas Children's Hospital, Houston, TX 77030, USA., Schweikhard V; Department of Bioengineering, Rice University, Houston, TX 77030, USA vs20@rice.edu diehl@rice.edu., Diehl MR; Department of Bioengineering, Rice University, Houston, TX 77030, USA vs20@rice.edu diehl@rice.edu.; Department of Chemistry, Rice University, Houston, TX 77030, USA.
Jazyk:	angličtina
Zdroj:	Biology open [Biol Open] 2017 Jun 15; Vol. 6 (6), pp. 785-799. Date of Electronic Publication: 2017 Jun 15.
DOI:	10.1242/bio.022624
Abstrakt:	IQGAP1 is a large, multi-domain scaffold that helps orchestrate cell signaling and cytoskeletal mechanics by controlling interactions among a spectrum of receptors, signaling intermediates, and cytoskeletal proteins. While this coordination is known to impact cell morphology, motility, cell adhesion, and vesicular traffic, among other functions, the spatiotemporal properties and regulatory mechanisms of IQGAP1 have not been fully resolved. Herein, we describe a series of super-resolution and live-cell imaging analyses that identified a role for IQGAP1 in the regulation of an actin cytoskeletal shell surrounding a novel membranous compartment that localizes selectively to the basal cortex of polarized epithelial cells (MCF-10A). We also show that IQGAP1 appears to both stabilize the actin coating and constrain its growth. Loss of compartmental IQGAP1 initiates a disassembly mechanism involving rapid and unconstrained actin polymerization around the compartment and dispersal of its vesicle contents. Together, these findings suggest IQGAP1 achieves this control by harnessing both stabilizing and antagonistic interactions with actin. They also demonstrate the utility of these compartments for image-based investigations of the spatial and temporal dynamics of IQGAP1 within endosome-specific actin networks. Competing Interests: Competing interestsThe authors declare no competing or financial interests. (© 2017. Published by The Company of Biologists Ltd.)
Databáze:	MEDLINE
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