TY  - GEN
T1  - Visualization of binding patterns for five Leucine-rich repeat proteins in the Drosophila embryo
AU  - Bali, Namrata
AU  - Zinn, Kai
DO  - 10.17912/micropub.biology.000199
UR  - http://beta.micropublication.org/journals/biology/micropub-biology-000199/
AB  - Leucine-rich repeat (LRR) domain-containing proteins play central roles in organizing neural connectivity. The LRR is a protein-recognition motif and proteins with extracellular LRR (eLRR) domains mediate intercellular communication and cell adhesion, which in turn regulate neuronal processes such as axon guidance, target selection, synapse formation and stabilization of connections (de Wit et al. 2011). The LRR-domain containing Slits and their Robo receptors are one of the best characterized examples of ligand-receptor pairs that regulate midline crossing and axon guidance in both Drosophila and vertebrates (Brose et al. 1999; Dickson and Gilestro 2006). There are 66 eLRR proteins in Drosophila, many of which are expressed in the nervous system and exhibit strikingly specific expression patterns, often labeling distinct subpopulations of neurons (Lauren et al. 2003; Dolan et al. 2007). The binding partners and functions of many of these eLRR proteins remain unknown.
PY  - 2019
JO  - microPublication Biology
ER  -