English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

alpha B-Crystallin, one of the small heat shock proteins, is constitutively expressed in lens as well as in nonlenticular tissues. It can function as a molecular chaperone for other lens crystallins and some other proteins. Its nonocular function is unknown although some reported one of them is related to cytoskeletal networks and/or components. In the present study, we demonstrate the association of alpha B-crystallin with tubulin. Immunoprecipitation experiments using L6 myoblast cell lysate with anti-alpha B-crystallin antibody resulted in the coprecipitation of alpha-tubulin, which was apparently temperature-dependent. Further, purified alpha B-crystallin prevented the turbidity development of purified tubulin molecule at 37 degrees C in vitro. Sucrose gradient centrifugation revealed that this chaperone activity was accompanied by the formation of large complex of alpha B-crystallin and tubulin dimer. These results indicate that one of the nonlenticular functions of alpha B-crystallin may be the protection of tubulin subunits of microtubules.

Chaperone Activity of .ALPHA.B-crystallin Suppresses Tubulin Aggregation through Complex Formation.