| First Author | Osseni A | Year | 2016 |
| Journal | J Cell Sci | Volume | 129 |
| Issue | 20 | Pages | 3744-3755 |
| PubMed ID | 27562070 | Mgi Jnum | J:247120 |
| Mgi Id | MGI:5923880 | Doi | 10.1242/jcs.188862 |
| Citation | Osseni A, et al. (2016) Triadin and CLIMP-63 form a link between triads and microtubules in muscle cells. J Cell Sci 129(20):3744-3755 |
| abstractText | 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. |
