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Compartmentalized NRG signaling and PDZ domain‐containing proteins in synapse structure and function
Author(s) -
Huang Yang Z.,
Wang Qiang,
Won Sandra,
Luo Zhen G.,
Xiong Wen C.,
Mei Lin
Publication year - 2002
Publication title -
international journal of developmental neuroscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.761
H-Index - 88
eISSN - 1873-474X
pISSN - 0736-5748
DOI - 10.1016/s0736-5748(02)00011-4
Subject(s) - agrin , pdz domain , neuregulin , microbiology and biotechnology , erbb , erbb4 , receptor tyrosine kinase , biology , signal transducing adaptor protein , neuromuscular junction , synapse , acetylcholine receptor , signal transduction , receptor , neuroscience , biochemistry
The synapse‐specific synthesis of the acetylcholine receptor (AChR) is mediated by multiple mechanisms including compartmentalized signaling induced by neuregulin (NRG). This paper presents evidence that NRG receptors—ErbB receptor tyrosine kinases interact with distinct PDZ domain‐containing proteins that are localized at the neuromuscular junction (NMJ). ErbB4 associates with the PSD‐95 (also known as SAP90)‐family members including PSD‐95, SAP97, and SAP102 whereas ErbB2 interacts with Erbin and PICK1. Although, ErbB kinases are concentrated at the NMJ, they are not colocalized with the AChR in cultured muscle cells even in the presence of agrin. Co‐expression of PSD‐95 causes ErbB4 to form clusters in COS cells. We propose that PDZ domain‐containing proteins play a role in anchoring ErbB proteins at the neuromuscular junction, and/or mediating downstream signaling pathways. Such mechanisms could be important for the maintenance and function of the synapse.