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The Roles of Actin-Binding Domains 1 and 2 in the Calcium-Dependent Regulation of Actin Filament Bundling by Human Plastins.

Abstract：

:The actin cytoskeleton is a complex network controlled by a vast array of intricately regulated actin-binding proteins. Human plastins (PLS1, PLS2, and PLS3) are evolutionary conserved proteins that non-covalently crosslink actin filaments into tight bundles. Through stabilization of such bundles, plastins contribute, in an isoform-specific manner, to the formation of kidney and intestinal microvilli, inner ear stereocilia, immune synapses, endocytic patches, adhesion contacts, and invadosomes of immune and cancer cells. All plastins comprise an N-terminal Ca2+-binding regulatory headpiece domain followed by two actin-binding domains (ABD1 and ABD2). Actin bundling occurs due to simultaneous binding of both ABDs to separate actin filaments. Bundling is negatively regulated by Ca2+, but the mechanism of this inhibition remains unknown. In this study, we found that the bundling abilities of PLS1 and PLS2 were similarly sensitive to Ca2+ (pCa50 ~6.4), whereas PLS3 was less sensitive (pCa50 ~5.9). At the same time, all three isoforms bound to F-actin in a Ca2+-independent manner, suggesting that binding of only one of the ABDs is inhibited by Ca2+. Using limited proteolysis and mass spectrometry, we found that in the presence of Ca2+ the EF-hands of human plastins bound to an immediately adjacent sequence homologous to canonical calmodulin-binding peptides. Furthermore, our data from differential centrifugation, Förster resonance energy transfer, native electrophoresis, and chemical crosslinking suggest that Ca2+ does not affect ABD1 but inhibits the ability of ABD2 to interact with actin. A structural mechanism of signal transmission from Ca2+ to ABD2 through EF-hands remains to be established.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Schwebach CL,Agrawal R,Lindert S,Kudryashova E,Kudryashov DS

doi

10.1016/j.jmb.2017.06.021

subject

Has Abstract

pub_date

2017-08-04 00:00:00

pages

2490-2508

issue

16

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(17)30322-4

journal_volume

429

pub_type

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