Ankyrin-B directs membrane tethering of periaxin and is required for maintenance of lens fiber cell hexagonal shape and mechanics.

Journal Article (Journal Article)

Periaxin (Prx), a PDZ domain protein expressed preferentially in myelinating Schwann cells and lens fibers, plays a key role in membrane scaffolding and cytoarchitecture. Little is known, however, about how Prx is anchored to the plasma membrane. Here we report that ankyrin-B (AnkB), a well-characterized adaptor protein involved in linking the spectrin-actin cytoskeleton to integral membrane proteins, is required for membrane association of Prx in lens fibers and colocalizes with Prx in hexagonal fiber cells. Under AnkB haploinsufficiency, Prx accumulates in the soluble fraction with a concomitant loss from the membrane-enriched fraction of mouse lenses. Moreover, AnkB haploinsufficiency induced age-dependent disruptions in fiber cell hexagonal geometry and radial alignment and decreased compressive stiffness in mouse lenses parallel to the changes observed in Prx null mouse lens. Both AnkB- and Prx-deficient mice exhibit disruptions in membrane organization of the spectrin-actin network and the dystrophin-glycoprotein complex in lens fiber cells. Taken together, these observations reveal that AnkB is required for Prx membrane anchoring and for maintenance of lens fiber cell hexagonal geometry, membrane skeleton organization, and biomechanics.

Full Text

Duke Authors

Cited Authors

  • Maddala, R; Walters, M; Brophy, PJ; Bennett, V; Rao, PV

Published Date

  • January 15, 2016

Published In

Volume / Issue

  • 310 / 2

Start / End Page

  • C115 - C126

PubMed ID

  • 26538089

Pubmed Central ID

  • PMC4719034

Electronic International Standard Serial Number (EISSN)

  • 1522-1563

Digital Object Identifier (DOI)

  • 10.1152/ajpcell.00111.2015


  • eng

Conference Location

  • United States