Trans-synaptic Adhesions between Netrin-G Ligand-3 (NGL-3) and Receptor Tyrosine Phosphatases LAR, Protein-tyrosine Phosphatase δ (PTPδ), and PTPσ via Specific Domains Regulate Excitatory Synapse Formation

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Trans-synaptic Adhesions between Netrin-G Ligand-3 (NGL-3) and Receptor Tyrosine Phosphatases LAR, Protein-tyrosine Phosphatase (PTP ), and PTP via Specific Domains Regulate Excitatory Synapse Formation*

Seok-Kyu Kwon, Jooyeon Woo, Soo-Young Kim, Hyun Kim, and Eunjoon Kim From the National Creative Research Initiative Center for Synaptogenesis, Department of Biological Sciences, and Department of Nanoscience and Technology, Korea Advanced Institute of Science and Technology, Daejeon 305-701 and the Department of Anatomy and Division of Brain Korea 21 Biomedical Science, College of Medicine, Kor...

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SALM5 trans-synaptically interacts with LAR-RPTPs in a splicing-dependent manner to regulate synapse development

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LAR protein tyrosine phosphatase regulates focal adhesions through CDK1.

Focal adhesions are complex multi-molecular structures that link the actin cytoskeleton to the extracellular matrix through integrin adhesion receptors and play a key role in regulation of many cellular functions. LAR (also known as PTPRF) is a receptor protein tyrosine phosphatase that regulates PDGF signalling and localises to focal adhesions. We have observed that loss of LAR phosphatase act...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 2010

ISSN: 0021-9258

DOI: 10.1074/jbc.m109.061127