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Neefjes-Mol , Anneke I. Letteboer , Jan Klooster , Frans P. CRB1 is thought to organize an intracellular protein scaffold in the retina that is involved in photoreceptor polarity.
This study was focused on the identification, subcellular localization, and binding characteristics of a novel member of the protein scaffold connected to CRB1.
To dissect the protein scaffold connected to CRB1, the yeast two-hybrid approach was used to screen for interacting proteins. Glutathione S -transferase GST pull-down analysis and immunoprecipitation were used to verify protein—protein interactions. The subcellular localization of the proteins was visualized by immunohistochemistry and confocal microscopy on human retinas and immunoelectron microscopy on mouse retinas.
These data imply that MPP4 and -5 have a role in photoreceptor polarity and, by association with CRB1, pinpoint the cognate genes as functional candidate genes for inherited retinopathies. Purchase this article with an account. Jump To Materials and Methods Results Discussion. Neefjes-Mol ; Anneke I. Letteboer ; Jan Klooster ; Frans P. Cremers ; Ronald Roepman ; Jan Wijnholds. Author Affiliations. Alerts User Alerts. You will receive an email whenever this article is corrected, updated, or cited in the literature.