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General Information:
Id:
13,395
Diseases:
Ciliopathy
Homo sapiens
article
Reference:
Lu H et al.(2017) Mutations in DZIP1L, which encodes a ciliary-transition-zone protein, cause autosomal recessive polycystic kidney disease Nat Genet 49: 1025-1034
[PMID: 28530676]
Interaction Information:
Comment
Mutations in DZIP1L, which encodes a ciliary-transition-zone protein, cause autosomal recessive polycystic kidney disease.
DZIP1L co-localizes with the transition zone protein tectonic 1 (TCTN1) in ciliated human fibroblasts. This was confirmed in retinal pigment epithelium (RPE-1) cells.
To further explore a function for DZIP1L at the cilium, the authors used human DZIP1L as bait to screen for interacting proteins in yeast two-hybrid libraries of highly ciliated human tissues (testis, lung and brain). From all three libraries, SEPT2 was identified as a high confidence interactor of DZIP1L. Septins are cytoskeletal GTPases, and SEPT2 functions as part of the periciliary diffusion barrier at the transition zone. The interaction was verified by co-immunoprecipitation of epitope-tagged DZIP1L and SEPT2 from transfected HEK293T cells, and by co-IP of the endogenous proteins from RPE-1 cells. Moreover, immunostaining of human dermal fibroblasts showed co-localization of DZIP1L and SEPT2 at the ciliary base.
In control human fibroblasts we detected PC1 at the basal body and along the axoneme, whereas there was a reduction in PC1 accumulation along the ciliary membrane of fibroblasts from individual B155. PC2 ciliary membrane localization was similarly affected in B155 fibroblasts. This suggests that in the absence of correct DZIP1L function, the ciliary membrane distribution of PC1 and PC2 is compromised, possibly reflecting a defect in the barrier function of the transition zone.
In control human fibroblasts we detected PC1 at the basal body and along the axoneme, whereas there was a reduction in PC1 accumulation along the ciliary membrane of fibroblasts from individual B155. PC2 ciliary membrane localization was similarly affected in B155 fibroblasts. This suggests that in the absence of correct DZIP1L function, the ciliary membrane distribution of PC1 and PC2 is compromised, possibly reflecting a defect in the barrier function of the transition zone.
In control human fibroblasts we detected PC1 at the basal body and along the axoneme, whereas there was a reduction in PC1 accumulation along the ciliary membrane of fibroblasts from individual B155. PC2 ciliary membrane localization was similarly affected in B155 fibroblasts. This suggests that in the absence of correct DZIP1L function, the ciliary membrane distribution of PC1 and PC2 is compromised, possibly reflecting a defect in the barrier function of the transition zone.
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