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

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Synaptic cell adhesion molecules regulate various steps of synapse formation. The trans-synaptic adhesion between postsynaptic NGL-3 (for netrin-G ligand-3) and presynaptic LAR (for leukocyte antigen-related) regulates excitatory synapse formation in a bidirectional manner. However, little is known about the molecular details of the NGL-3-LAR adhesion and whether two additional LAR family proteins, protein-tyrosine phosphatase delta (PTP delta), and PTP sigma, also interact with NGL-3 and are involved in synapse formation. We report here that the leucine-rich repeat (LRR) domain of NGL-3, containing nine LRRs, interacts with the first two fibronectin III (FNIII) domains of LAR to induce bidirectional synapse formation. Moreover, Gln-96 in the first LRR motif of NGL-3 is critical for LAR binding and induction of presynaptic differentiation. PTP delta and PTP sigma also interact with NGL-3 via their first two FNIII domains. These two interactions promote synapse formation in a different manner; the PTP sigma-NGL-3 interaction promotes synapse formation in a bidirectional manner, whereas the PTP delta-NGL-3 interaction instructs only presynaptic differentiation in a unidirectional manner. mRNAs encoding LAR family proteins display overlapping and differential expression patterns in various brain regions. These results suggest that trans-synaptic adhesion between NGL-3 and the three LAR family proteins regulates excitatory synapse formation in shared and distinct neural circuits.
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Issue Date
2010-04
Language
English
Article Type
Article
Keywords

LEUCINE-RICH REPEAT; HIPPOCAMPAL CHOLINERGIC INNERVATION; CENTRAL-NERVOUS-SYSTEM; LIPRIN-ALPHA; MICE LACKING; SYNAPTOGENIC PROTEINS; SULFATE PROTEOGLYCAN; DEFICIENT MICE; ACTIVE ZONE; RPTP-DELTA

Citation

JOURNAL OF BIOLOGICAL CHEMISTRY, v.285, no.18, pp.13966 - 13978

ISSN
0021-9258
DOI
10.1074/jbc.M109.061127
URI
http://hdl.handle.net/10203/97590
Appears in Collection
BS-Journal Papers(저널논문)
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