Self-recognition at the atomic level: understanding the astonishing molecular diversity of homophilic Dscams.
The Drosophila Dscams are immunoglobulin superfamily members produced from a single gene that is diversified by alternative splicing to produce a family of cell-surface proteins with over 19,000 different ectodomain isoforms. Dscams are critical for neuronal wiring, and mounting evidence suggests that they play a key role in self-avoidance between sister branches from neurons, which depends on homophilic self-recognition by Dscams. Two recent papers shed new light on Dscam recognition: first by showing that the vast majority of Dscam isoforms mediate specific homophilic binding and second by revealing the essence of the molecular basis of homophilic recognition by Dscams through high-resolution structural studies.
Shapiro
Lawrence
L
Department of Biochemistry and Molecular Biophysics and Edward S Harkness Eye Institute, Columbia University, New York, NY 10032, USA. lss8@columbia.edu
D017398:Alternative Splicing; D000818:Animals; D015815:Cell Adhesion Molecules; D004330:Drosophila; D029721:Drosophila Proteins / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D009474:Neurons / Q000378:metabolism*
D015815:Cell Adhesion Molecules; D029721:Drosophila Proteins; C491736:Dscam1 protein, Drosophila