Research article summary (published 26 Mar 2002):

Drosophila liprin-alpha and the receptor phosphatase Dlar control synapse morphogenesis.

Full Abstract

Here, we examine the synaptic function of the receptor protein tyrosine phosphatase (RPTP), Dlar, and an associated intracellular protein, Dliprin-alpha, at the Drosophila larval neuromuscular junction. We show that Dliprin-alpha and Dlar are required for normal synaptic morphology. We also find that synapse complexity is proportional to the amount of Dlar gene product, suggesting that Dlar activity determines synapse size. Ultrastructural analysis reveals that Dliprin-alpha and Dlar are required to define the size and shape of the presynaptic active zone. Accordingly, there is a concomitant decrease in synaptic transmission in both mutants. Finally, epistasis analysis indicates that Dliprin-alpha is required for Dlar's action at the synapse. These data suggest a model where Dliprin-alpha and Dlar cooperate to regulate the formation and/or maintenance of a network of presynaptic proteins.

Author information

Author/s: Kaufmann, Nancy (N); DeProto, Jamin (J); Ranjan, Ravi (R); Wan, Hong (H); Van Vactor, David (D);

Affiliation: Department of Cell Biology, Program in Neuroscience and DFCI/Harvard Cancer Center, Harvard Medical School, Boston, MA 02115, USA.

Grants: NS 35909 (Agency:NINDS NIH HHS) ; NS 40043 (Agency:NINDS NIH HHS)

Journal and publication information

Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S.

Journal: Neuron (Neuron), published in United States. (Language: eng)

Reference: 2002-Mar; vol 34 (issue 1) : pp 27-38

Dates: Created 2002/04/04; Completed 2002/04/29; Revised 2007/11/15;

PMID: 11931739, status: MEDLINE (last retrieval date: 2/18/2009, IMS Date: )

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

Comments and Corrections

CommentIn: Neuron. 2002 Mar 28;34(1):1-2. (PMID: 11931733)

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MeSH headings (categories)

This article was linked to the MESH Headings shown below.

Adaptor Proteins, Signal Transducing Amino Acid Sequence - genetics Animals Drosophila - embryology; enzymology; genetics; physiology Drosophila Proteins - genetics; physiology Humans Male Molecular Sequence Data

Molecular Sequence Data Morphogenesis - physiology Mutation - genetics Neuromuscular Junction - enzymology; genetics; growth & development; physiology Phosphoproteins - genetics; physiology Protein Tyrosine Phosphatases - genetics; physiology Receptor-Like Protein Tyrosine Phosphatases Synapses - enzymology; genetics; physiology; ultrastructure

Associated Chemicals: Adaptor Proteins, Signal Transducing (0) ; Drosophila Proteins (0) ; Liprin-alpha protein, Drosophila (0) ; PPFIA1 protein, human (0) ; Phosphoproteins (0) ; Lar protein, Drosophila (EC 3.1.3.48) ; Protein Tyrosine Phosphatases (EC 3.1.3.48) ; Receptor-Like Protein Tyrosine Phosphatases (EC 3.1.3.48)

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