Abstract：
:Dscam1 potentially encodes 19,008 ectodomains of a cell recognition molecule of the immunoglobulin (Ig) superfamily through alternative splicing. Each ectodomain, comprising a unique combination of three variable (Ig) domains, exhibits isoform-specific homophilic binding in vitro. Although we have proposed that the ability of Dscam1 isoforms to distinguish between one another is crucial for neural circuit assembly, via a process called self-avoidance, whether recognition specificity is essential in vivo has not been addressed. Here we tackle this issue by assessing the function of Dscam1 isoforms with altered binding specificities. We generated pairs of chimeric isoforms that bind to each other (heterophilic) but not to themselves (homophilic). These isoforms failed to support self-avoidance or did so poorly. By contrast, coexpression of complementary isoforms within the same neuron restored self-avoidance. These data establish that recognition between Dscam1 isoforms on neurites of the same cell provides the molecular basis for self-avoidance.
journal_name
Neuronjournal_title
Neuronauthors
Wu W,Ahlsen G,Baker D,Shapiro L,Zipursky SLdoi
10.1016/j.neuron.2012.02.029subject
Has Abstractpub_date
2012-04-26 00:00:00pages
261-8issue
2eissn
0896-6273issn
1097-4199pii
S0896-6273(12)00266-8journal_volume
74pub_type
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