Abstract
Purpose :
PRCD is a unique photoreceptor disc component, which is involved in outer segment disc formation. The purpose of this work was to identify PRCD-binding proteins in the retina.
Methods :
PRCD protein-protein interactions were identified implementing the Ras Recruitment System (RRS), a cytoplasmic-based yeast two-hybrid system, on a bovine retina cDNA library. Identified interactions were confirmed by co-immunoprecipitation. Immunostaining was used to test the effect of PRCD interactions in the murine retina.
Results :
We identified an interaction of PRCD with Tubby-like protein 1 (TULP1). Co-immunoprecipitation in transfected mammalian cells confirmed that PRCD interacts with TULP1, as well as with its homolog, TUB. These interactions were mediated by TULP1 and TUB highly conserved C-terminal tubby domain. PRCD localization was altered in retinas of TULP1-deficient mice.
Conclusions :
PRCD is a unique photoreceptor disc component. Our results show that TULP1, which is involved in the vesicular trafficking of several photoreceptor proteins from the inner segment to the outer segment, is required for PRCD exclusive localization to photoreceptor outer segment discs.
This is a 2020 ARVO Annual Meeting abstract.