anti-ADP-Ribosylation Factor-Like 13B (ARL13B) Antibodies

Zebrafish ADP-Ribosylation Factor-Like 13B (ARL13B) interaction partners

1. Between 2 and 5 days post fertilization (dpf), arl13b is expressed in neural tissues while expression of arl13a is downregulated by 2 dpf and restricted to craniofacial structures. These results indicate that arl13a and arl13b have evolved different roles and that arl13a does not function in the zebrafish retina.

2. loss of Arl13b leads to slow photoreceptor degeneration, but can be exacerbated by the loss of vangl2. Importantly, the data show that Arl13b can genetically and physically interact with Vangl2 and this association is important for normal photoreceptor structure.

3. Arl13b is an important effector of ciliary membrane biogenesis and ciliary length regulation.

4. Cilia localization is essential for in vivo functions of the Joubert syndrome protein arl13b.

Human ADP-Ribosylation Factor-Like 13B (ARL13B) interaction partners

1. Joubert syndrome protein ARL13B controls axoneme polyglutamylation.

2. A novel homozygous loss of function mutation in ARL13B was identified in patients with Joubert syndrome

3. High Arl13b expression is associated with medulloblastoma formation.

4. the results show that palmitoylation plays a unique and critical role in controlling the localization, stability, abundance, and thus function of ARL13b. Pharmacological manipulation of protein palmitoylation may be a strategy to alter cilia function.

5. Our results show how Arl13b participates in Hedgehog pathway activation in gastric cancer

6. Reduced primary cilia length and altered Arl13b expression are associated with deregulated chondrocyte Hedgehog signaling in alkaptonuria.

7. ARL13B regulates IFT-A-mediated retrograde protein trafficking within cilia through its interaction with INPP5E.

8. Biochemical characterization of purified mammalian ARL13B protein indicates that it is an atypical GTPase and ARL3 guanine nucleotide exchange factor (GEF).(

9. Thus our data identify a novel ARL13B variant that causes JS and retinopathy and suggest an extension of the phenotypic spectrum of ARL13B mutations to obesity.

10. We conclude that MKS/NPHP modules comprise a TZ barrier to ARL-13 diffusion, whereas IFT genes predominantly facilitate ARL-13 ciliary entry and/or retention via active transport mechanisms.

11. X-ray crystallography of Arl13B demonstrates involvement of mutations R79Q and R200C in stabilizing intramolecular interactions.

12. Arl13b acts as the all-rounder in cilia formation and signaling (Review).

13. findings indicate that ARL13B, INPP5E, PDE6D, and CEP164 form a distinct functional network that is involved in JBTS and NPHP but independent of the ones previously defined by NPHP and MKS proteins

14. data reveal a novel but conserved role for the SUMOylation modification of ciliary small GTPase ARL13B in specifically regulating the proper ciliary targeting of various sensory receptors

15. These results indicate a previously unidentified role for Arl13b in endocytic recycling traffic and suggest a link between Arl13b function and the actin cytoskeleton.

16. Expression of Arl13b variants known to cause Joubert syndrome induce defective interneuronal migration, suggesting that defects in cilia-dependent interneuron migration may in part underlie the neurological defects in Joubert syndrome patients.

17. data implicate a role for JS-associated Arl13b at ciliary membranes, where it regulates ciliary transmembrane protein localizations and anterograde IFT assembly stability

18. These findings suggest that N and C domains of Arl13b cooperatively regulate its ciliary localization and that N domain-dependent self-association of Arl13b may be important for its function in cilia biogenesis.

19. ARL13B has an evolutionarily conserved role mediating cilia function in multiple organs

Mouse (Murine) ADP-Ribosylation Factor-Like 13B (ARL13B) interaction partners

1. High Arl13b expression is associated with medulloblastoma formation.

2. Arl13b dysfunction resulted in hennin cell stagnation due to poor growth factor signaling and impaired detection of extracellular electrical gradients.

3. Biochemical characterization of purified mammalian ARL13B protein indicates that it is an atypical GTPase and ARL3 guanine nucleotide exchange factor (GEF).(

4. To investigate whether Arl13b has a role in ciliogenesis in mammalian kidney and whether loss of function of Arl13b leads to cystic kidneys in mammals, we generated a mouse model with kidney-specific conditional knockout of Arl13b Deletion of Arl13b in the distal nephron at the perinatal stage led to a cilia biogenesis defect and rapid kidney cyst formation

5. The authors show that the ciliary G-protein Arl13B, mutated in Joubert syndrome, is the guanine nucleotide exchange factor for Arl3, and its function is conserved in evolution

6. A new role for Arl13b in actin cytoskeleton remodeling through the interaction with Myh9.

7. Early neuroepithelial deletion of ciliary Arl13b reversed the apical-basal polarity of radial progenitors & caused aberrant neuronal placement. Arl13b signaling in primary cilia is crucial for initial formation of a polarized radial glial scaffold.

8. guidance cue receptors essential for interneuronal migration localize to interneuronal primary cilia, but their concentration and dynamics are altered in the absence of Arl13b

9. By deleting Arl13b in mouse, we induced low-level constitutive GliA function at specific developmental stages and defined a crucial period prior to E10.5 when shifts in the level of GliA cause cells to change their fate

10. Study shows the cilia protein Arl13b is required for left right axis specification as its absence results in heterotaxia; the defect originates in the node where Cerl2 is not downregulated and asymmetric expression of Nodal is not maintained resulting in symmetric expression of both genes.

11. The role of Arl13b in ciliogenesis and it's interaction with Smo and Shh proteins.Arl13b regulates the ciliary entry of Smo.

12. Arl13bhnn mutants have abnormal ventral neural tube patterning due to disrupted sonic hedgehog signaling; in addition, dorsal patterning defects occur from abnormal bone morphogenetic protein signaling.