Abstract：
:In skeletal muscle, the triad is a structure comprising a transverse (T)-tubule and sarcoplasmic reticulum (SR) cisternae. Triads constitute the basis of excitation-contraction coupling as the cradle of the Ca2+ release complex. We have shown previously that triadin, a member of this complex, has shaping properties on reticulum membrane and is indirectly involved in a link between triads and microtubules. We have identified here that CLIMP-63 (also known as CKAP4), as the partner of triadin, is responsible for this association of triads and microtubules. Triadin and CLIMP-63 interact through their respective luminal domains and the shaping properties of triadin depend on the capacity of CLIMP-63 to bind microtubules with its cytosolic portion. In skeletal muscle, CLIMP-63 is localized in the SR, including triads, and is associated with the Ca2+ release complex through its interaction with triadin. Knockout of triadin in muscles results in the delocalization of CLIMP-63 from triads, its dissociation from the Ca2+ release complex and a disorganization of the microtubule network. Our results suggest that the association of triadin and CLIMP-63 could be involved in the shaping of SR terminal cisternae and in the guidance of microtubules close to the triads.
journal_name
J Cell Scijournal_title
Journal of cell scienceauthors
Osseni A,Sébastien M,Sarrault O,Baudet M,Couté Y,Fauré J,Fourest-Lieuvin A,Marty Idoi
10.1242/jcs.188862subject
Has Abstractpub_date
2016-10-15 00:00:00pages
3744-3755issue
20eissn
0021-9533issn
1477-9137pii
jcs.188862journal_volume
129pub_type
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