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J Cell Sci. 2016 Oct 15;129(20):3744-3755. Epub 2016 Aug 25.

Triadin and CLIMP-63 form a link between triads and microtubules in muscle cells.

Author information

1
University Grenoble Alpes, Grenoble Institut des Neurosciences, GIN, Grenoble F-38000, France INSERM, U1216, Grenoble F-38000, France.
2
University Grenoble Alpes, BIG-BGE, Grenoble F-38000, France CEA, BIG, BGE and GPC, Grenoble F-38000, France INSERM, BGE, Grenoble F-38000, France.
3
University Grenoble Alpes, Grenoble Institut des Neurosciences, GIN, Grenoble F-38000, France INSERM, U1216, Grenoble F-38000, France CHU de Grenoble, Grenoble F-38000, France.
4
University Grenoble Alpes, Grenoble Institut des Neurosciences, GIN, Grenoble F-38000, France INSERM, U1216, Grenoble F-38000, France CEA, BIG, BGE and GPC, Grenoble F-38000, France isabelle.marty@univ-grenoble-alpes.fr anne.fourest-lieuvin@univ-grenoble-alpes.fr.
5
University Grenoble Alpes, Grenoble Institut des Neurosciences, GIN, Grenoble F-38000, France INSERM, U1216, Grenoble F-38000, France isabelle.marty@univ-grenoble-alpes.fr anne.fourest-lieuvin@univ-grenoble-alpes.fr.

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.

KEYWORDS:

CLIMP-63; Ca2+ release complex; Microtubule; Sarcoplasmic reticulum; Triad; Triadin

PMID:
27562070
DOI:
10.1242/jcs.188862
[Indexed for MEDLINE]
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