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EPLIN-α and -β Isoforms Modulate Endothelial Cell Dynamics through a Spatiotemporally Differentiated Interaction with Actin.
Taha, Muna Aldirawi, Mohammed März, Sigrid Seebach, Jochen Odenthal-Schnittler, Maria Bondareva, Olga Bojovic, Vesna Schmandra, Thomas Wirth, Benedikt Mietkowska, Magdalena
Taha, Muna
Aldirawi, Mohammed
März, Sigrid
Seebach, Jochen
Odenthal-Schnittler, Maria
Bondareva, Olga
Bojovic, Vesna
Schmandra, Thomas
Wirth, Benedikt
Mietkowska, Magdalena
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2019-10-22
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Abstract
Actin-binding proteins are essential for linear and branched actin filament dynamics that control shape change, cell migration, and cell junction remodeling in vascular endothelium (endothelial cells [ECs]). The epithelial protein lost in neoplasm (EPLIN) is an actin-binding protein, expressed as EPLIN-α and EPLIN-β by alternative promoters; however, the isoform-specific functions are not yet understood. Aortic compared to cava vein ECs and shear stress-exposed cultured ECs express increased EPLIN-β levels that stabilize stress fibers. In contrast, EPLIN-α expression is increased in growing and migrating ECs, is targeted to membrane protrusions, and terminates their growth via interaction with the Arp2/3 complex. The data indicate that EPLIN-α controls protrusion dynamics while EPLIN-β has an actin filament stabilizing role, which is consistent with FRAP analyses demonstrating a lower EPLIN-β turnover rate compared to EPLIN-α. Together, EPLIN isoforms differentially control actin dynamics in ECs, essential in shear stress responses, cell migration, and barrier function.
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Cell Rep. 2019 Oct 22;29(4):1010-1026.e6. doi: 10.1016/j.celrep.2019.09.043.
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en
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2211-1247
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Attribution-NonCommercial-ShareAlike 4.0 International