Chelicerata Sdscam Isoforms Combine Homophilic Specificities to Define Unique Cell Recognition
Chelicerata sDscam isoforms combine homophilic specificities to define unique cell recognition Fengyan Zhoua, Guozheng Caoa, Songjun Daia, Guo Lia, Hao Lia, Zhu Dinga, Shouqing Houa, Bingbing Xua, Wendong Youb, Gil Wiseglassc, Feng Shia, Xiaofeng Yangb, Rotem Rubinsteinc, and Yongfeng Jina,b,1 aMOE Laboratory of Biosystems Homeostasis & Protection, Innovation Center for Cell Signaling Network, College of Life Sciences, Zhejiang University, ZJ310058 Hangzhou, Zhejiang, China; bDepartment of Neurosurgery, First Affiliated Hospital, School of Medicine, Zhejiang University, ZJ310058 Hangzhou, Zhejiang, China; and cSchool of Neurobiology, Biochemistry and Biophysics, Sagol School of Neuroscience, George S. Wise Faculty of Life Science, Tel Aviv University, 69978 Ramat Aviv, Israel Edited by Barry Honig, Howard Hughes Medical Institute, Columbia University, New York, NY, and approved August 20, 2020 (received for review December 15, 2019) Thousands of Down syndrome cell adhesion molecule (Dscam1) (13–16). Different isoforms share the same domain organization isoforms and ∼60 clustered protocadhrein (cPcdh) proteins are re- with 10 Ig domains, 6 fibronectin type III (FNIII) domains, a quired for establishing neural circuits in insects and vertebrates, single transmembrane (TM) region, and a cytoplasmic domain, respectively. The strict homophilic specificity exhibited by these but differ in the primary sequences of at least 1 of 3 Ig domains. proteins has been extensively studied and is thought to be critical Individual neuronal identities are determined by the stochastic for their function in neuronal self-avoidance. In contrast, signifi- expression of a small set of 10 to 50 distinct Dscam1 isoforms of cantly less is known about the Dscam1-related family of ∼100 short- the tens of thousands of possible isoforms that can be generated ened Dscam (sDscam) proteins in Chelicerata.
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