TY - JOUR
AU - 
AB - Article Dual arginine recognition of LRRK2 phosphorylated Rab GTPases 1 2 3, Dieter Waschbusch, Elena Purlyte, and Amir R. Khan 1 2 School of Biochemistry and Immunology, Trinity College Dublin, Dublin, Ireland; MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, United Kingdom; and Division of Newborn Medicine, Boston Children’s Hospital, Boston, Massachusetts ABSTRACT Parkinson’s-disease-associated LRRK2 is a multidomain Ser/Thr kinase that phosphorylates a subset of Rab GTPases to control their effector functions. Rab GTPases are the prime regulators of membrane trafficking in eukaryotic cells. Rabs exert their biological effects by recruitment of effector proteins to subcellular compartments via their Rab-binding domain (RBD). Effectors are modular and typically contain additional domains that regulate various aspects of vesicle formation, trafficking, fusion, and organelle dynamics. The RBD of effectors is typically an a-helical coiled coil that recognizes the GTP conformation of the switch 1 and switch 2 motifs of Rabs. LRRK2 phosphorylates Rab8a at T72 (pT72) of its switch 2 a-helix. This post-translational modification enables recruitment of RILPL2, an effector that regulates ciliogenesis in model cell lines. A newly identified RBD motif of RILPL2, termed the X-cap, has been shown to recognize the phosphate via direct 
TI - Dual arginine recognition of LRRK2 phosphorylated Rab GTPases
JF - Biophysical Journal
DO - 10.1016/j.bpj.2021.03.030
DA - 2021-05-01
UR - https://www.deepdyve.com/lp/unpaywall/dual-arginine-recognition-of-lrrk2-phosphorylated-rab-gtpases-GcqG8MpJKr
DP - DeepDyve
ER -