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 Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Calcium is a crucial element for striated muscle function. As such, myoplasmic free Ca(2+) concentration is delicately regulated through the concerted action of multiple Ca(2+) pathways that relay excitation of the plasma membrane to the intracellular contractile machinery. In skeletal muscle, one of these major Ca(2+) pathways is Ca(2+) release from intracellular Ca(2+) stores through type-1 ryanodine receptor/Ca(2+) release channels (RyR1), which positions RyR1 in a strategic cross point to regulate Ca(2+) homeostasis. This major Ca(2+) traffic point appears to be highly sensitive to the intracellular environment, which senses through a plethora of chemical and protein-protein interactions. Among these modulators, perhaps one of the most elusive is Triadin, a muscle-specific protein that is involved in many crucial aspect of muscle function. This family of proteins mediates complex interactions with various Ca(2+) modulators and seems poised to be a relevant modulator of Ca(2+) signaling in cardiac and skeletal muscles. The purpose of this review is to examine the most recent evidence and current understanding of the role of Triadin in muscle function, in general, with particular emphasis on its contribution to Ca(2+) homeostasis.

On the footsteps of Triadin and its role in skeletal muscle