1H, 13C and 15N resonance assignments for Binder of Arl2, BART

Bailey, Laura K.; Campbell, Louise J.; Evetts, Katrina A.; Littlefield, Keily; Rajendra, Eeson; Nietlispach, Daniel; Owen, Darerca; Mott, Helen R.

doi:10.1007/s12104-008-9135-3

Cited by 1 publication

(1 citation statement)

References 7 publications

(5 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In contrast, despite having an NH 2 -terminal glycine (site of N-myristoylation), ARL2 is not myristoylated, and, despite having amphipathic ␣-helices at their NH 2 -termini, ARLs have not been shown to translocate onto membranes upon activation. Rather, the NH 2terminal helices (or at least residues found within them) have been found to make critical direct contact with effectors, essentially serving as a third effector loop in addition to the two canonical ones present in all regulatory GTPases (5,6,180). These NH 2 -terminal helices are also important in displacement of cargos bound to other binding partners (see below discussion of mechanisms of ARL3 and ARL2).…”

Section: Arf and Arlsmentioning

confidence: 99%

ARF family GTPases with links to cilia

Fisher

Kuna

Caspary

et al. 2020

American Journal of Physiology-Cell Physiology

View full text Add to dashboard Cite

The ARF superfamily of regulatory GTPases, including both the ARF and ARL proteins, control a multitude of cellular functions including aspects of vesicular traffic, lipid metabolism, mitochondrial architecture, the assembly and dynamics of the microtubule and actin cytoskeletons, and other pathways in cell biology. Considering their general utility, it is perhaps not surprising that increasingly ARF/ARLs have been found in connection to primary cilia. Here, we critically evaluate the current knowledge of the role four ARF/ARLs (ARF4, ARL3, ARL13B and ARL6) play in cilia and highlight key missing information that would help move our understanding forward. Importantly, these GTPases are themselves regulated by guanine nucleotide exchange factors (GEFs) that activate them and by GTPase activating proteins (GAPs) that act as both effectors and terminators of signaling. We believe that the identification of the GEFs and GAPs and better models of the actions of these GTPases and their regulators will provide a much deeper understanding and appreciation of the mechanisms that underly ciliary functions and the causes of a number of human ciliopathies.

show abstract

Section: Arf and Arlsmentioning

confidence: 99%