{'fraction_non_alphanumeric': 0.0572655690765927, 'fraction_numerical': 0.02791696492483894, 'mean_word_length': 5.213333333333333, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
PDE6D binds to the C‐terminus of RPGR in a prenylation‐dependent manner

Ciliary dysfunction underlies multiple human genetic diseases, and mechanisms of protein trafficking to cilia are an area of active investigation. PDE6D (also known as PDEδ and PrBP) is a prenyl‐binding protein involved in ciliary targeting of prenylated proteins [1], [2], [3], [4]. Previous studies uncovered that PDE6D interacts with RPGR [5], [6], mutations of which cause retinitis pigmentosa [7], [8], [9], [10]. More recently, the structure of the PDE6D and RPGR (the N‐terminal half) complex was determined and RPGR was proposed as a scaffold protein that recruits cargo‐loaded PDE6D to the ciliary base [6]. Here, we show an alternative mode of interaction between RPGR and PDE6D.

Two main isoforms of RPGR (RPGRex1–19 and RPGRORF15) are expressed in vertebrates [8], [11]. Of these, RPGRORF15 appears to be expressed specifically in photoreceptor cells, while RPGRex1–19 is expressed ubiquitously. The RPGRex1–19 isoform (hereafter RPGR) has the CaaX prenylation motif and is geranylgeranylated at its C‐terminus. The interaction between RPGR and PDE6D was initially discovered by a yeast two‐hybrid screen and further verified by an in vitro GST pull‐down assay [5], [6]. In these studies, PDE6D was found to interact with the RCC1‐like domain (RLD) within the N‐terminal half of RPGR. While we were conducting …