Abstract
Objective Pericentrin, a highly conserved protein of the pericentriolar material, serves as a multifunctional scaffold for numerous proteins and plays an important role in microtubule organization. Mutations in the human PCNT gene are associated with a range of diseases including primordial dwarfism and ciliopathies. In the mouse retina Pericentrin colocalizes with several proteins responsible for transport processes at the connecting cilium between the two photoreceptor compartments. In order to get more insights on the function of Pericentrin in the retina we try to identify new ciliary as well as centrosomal interaction partners.
Highlights
Identification of Pericentrin interaction partners was done by Tandem Affinity Purification, Yeast two-hybrid with a self-constructed cDNA library from mouse retina and GST pull-down
We were able to show that Pericentrin interacts with Klarsicht/ANC-1/Syne-homologue (KASH) domain-containing protein Syne-2
We found a partial colocalization of Pericentrin and Syne-2 in the ciliary region of mouse photoreceptors
Summary
Pericentrin, a highly conserved protein of the pericentriolar material, serves as a multifunctional scaffold for numerous proteins and plays an important role in microtubule organization. Mutations in the human PCNT gene are associated with a range of diseases including primordial dwarfism and ciliopathies. In the mouse retina Pericentrin colocalizes with several proteins responsible for transport processes at the connecting cilium between the two photoreceptor compartments. In order to get more insights on the function of Pericentrin in the retina we try to identify new ciliary as well as centrosomal interaction partners
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