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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 08 Dec 2016.

ADP-ribosylation factor-like 4D

ARL5, ARF4L, Arl4d
ADP-ribosylation factor 4D is a member of the ADP-ribosylation factor family of GTP-binding proteins. ARL4D is closely similar to ARL4A and ARL4C and each has a nuclear localization signal and an unusually high guanine nucleotide exchange rate. This protein may play a role in membrane-associated intracellular trafficking. Mutations in this gene have been associated with Bardet-Biedl syndrome (BBS). [provided by RefSeq, Jul 2008] (from NCBI)
Papers on ARL5
Bardet-Biedl syndrome 3 (Bbs3) knockout mouse model reveals common BBS-associated phenotypes and Bbs3 unique phenotypes.
Sheffield et al., Iowa City, United States. In Proc Natl Acad Sci U S A, 2012
Bbs3 knockout mouse model reveals common BBS-associated phenotypes and Bbs3 unique phenotypes
Overexpression of the small GTPase Arl4D suppresses adipogenesis.
Park et al., Ch┼Ćnju, South Korea. In Int J Mol Med, 2011
The results suggest that rapid reduction of Arl4D is required for adipogenesis to proceed.
Epistasis contributes to the genetic buffering of plasma HDL cholesterol in mice.
Churchill et al., Bar Harbor, United States. In Physiol Genomics, 2010
analysis identified an epistatic interaction that plays a role in the buffering of HDL levels in C57BL/6J mice, and we have identified Arl4d as a candidate gene that mediates this effect.
Identification and functional analysis of the vision-specific BBS3 (ARL6) long isoform.
Slusarski et al., Iowa City, United States. In Plos Genet, 2010
These data demonstrate that the BBS3L transcript is required for proper retinal function and organization.
Valproic acid-inducible Arl4D and cytohesin-2/ARNO, acting through the downstream Arf6, regulate neurite outgrowth in N1E-115 cells.
Tanoue et al., Tokyo, Japan. In Exp Cell Res, 2009
Arl4D is a previously unknown regulator of neurite formation through cytohesin-2 and Arf6, providing another example that the functional interaction of two different small GTPases controls an important cellular function.
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