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ARL13B encodes a member of the ADP-ribosylation factor-like family. Additionally we are shipping ARL13B Antibodies (26) and ARL13B Proteins (6) and many more products for this protein.
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Arl13b is an important effector of ciliary membrane biogenesis and ciliary length regulation.
Cilia localization is essential for in vivo functions of the Joubert syndrome protein arl13b.
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.
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.
X-ray crystallography of Arl13B demonstrates involvement of mutations R79Q and R200C in stabilizing intramolecular interactions.
Arl13b acts as the all-rounder in cilia formation and signaling (Review).
findings indicate that ARL13B, INPP5E (show PMPCA ELISA Kits), PDE6D (show PDE6D ELISA Kits), and CEP164 (show CEP164 ELISA Kits) form a distinct functional network that is involved in JBTS and NPHP but independent of the ones previously defined by NPHP and MKS (show MKS1 ELISA Kits) proteins
data reveal a novel but conserved role for the SUMOylation modification of ciliary small GTPase (show RACGAP1 ELISA Kits) ARL13B in specifically regulating the proper ciliary targeting of various sensory receptors
These results indicate a previously unidentified role for Arl13b in endocytic recycling traffic and suggest a link between Arl13b function and the actin cytoskeleton.
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.
data implicate a role for JS-associated Arl13b at ciliary membranes, where it regulates ciliary transmembrane protein localizations and anterograde IFT assembly stability
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.
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
A new role for Arl13b in actin cytoskeleton remodeling through the interaction with Myh9 (show MYH9 ELISA Kits).
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.
guidance cue receptors essential for interneuronal migration localize to interneuronal primary cilia, but their concentration and dynamics are altered in the absence of Arl13b
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
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 (show DAND5 ELISA Kits) is not downregulated and asymmetric expression of Nodal is not maintained resulting in symmetric expression of both genes.
The role of Arl13b in ciliogenesis and it's interaction with Smo and Shh proteins.Arl13b regulates the ciliary entry of Smo.
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.
This gene encodes a member of the ADP-ribosylation factor-like family. The encoded protein is a small GTPase that contains both N-terminal and C-terminal guanine nucleotide-binding motifs. This protein is localized in the cilia and plays a role in cilia formation and in maintenance of cilia. Mutations in this gene are the cause of Joubert syndrome 8. Alternate splicing results in multiple transcript variants.
ADP-ribosylation factor-like protein 13B
, ADP-ribosylation factor-like 2-like 1
, ADP-ribosylation factor-like 13B
, ADP-ribosylation factor-like protein 13B-like
, ADP-ribosylation factor-like protein 2-like 1
, ARL2-like protein 1
, protein scorpion
, un-named hi459
, unm hi459