The C. elegans LAR-like receptor tyrosine phosphatase PTP-3 and the VAB-1 Eph receptor tyrosine kinase have partly redundant functions in morphogenesis

Robert J Harrington; Michael J Gutch; Michael O Hengartner; Nicholas K Tonks; Andrew D Chisholm

doi:10.5167/uzh-946

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The C. elegans LAR-like receptor tyrosine phosphatase PTP-3 and the VAB-1 Eph receptor tyrosine kinase have partly redundant functions in morphogenesis

Journal article

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The C. elegans LAR-like receptor tyrosine phosphatase PTP-3 and the VAB-1 Eph receptor tyrosine kinase have partly redundant functions in morphogenesis

Robert J Harrington, Michael J Gutch, Michael O Hengartner, Nicholas K Tonks and Andrew D Chisholm

Development (Cambridge), Vol.129(9), pp.2141-2153

05/2002

DOI: https://doi.org/10.5167/uzh-946

Handle:

https://hdl.handle.net/2376/114570

PMID: 11959824

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Abstract

Protein Tyrosine Phosphatase, Non-Receptor Type 11

Genes, Helminth

Molecular Sequence Data

RNA, Messenger - metabolism

Morphogenesis

Protein Tyrosine Phosphatases - chemistry

Protein Tyrosine Phosphatases - genetics

RNA, Helminth - metabolism

Gene Expression Regulation, Developmental

Base Sequence

Cloning, Molecular

Helminth Proteins - physiology

Cell Cycle Proteins - genetics

RNA, Helminth - genetics

Amino Acid Sequence

Caenorhabditis elegans Proteins

Ephrins

Caenorhabditis elegans - growth & development

Animals, Genetically Modified

Caenorhabditis elegans - genetics

RNA, Messenger - genetics

Intracellular Signaling Peptides and Proteins

Helminth Proteins - genetics

Receptor Protein-Tyrosine Kinases

Sequence Homology, Amino Acid

Phenotype

Animals

Mutation

Cell Cycle Proteins - physiology

Caenorhabditis elegans - enzymology

Evolution, Molecular

Protein Tyrosine Phosphatases - physiology

Receptor-like protein-tyrosine phosphatases (RPTPs) form a diverse family of cell surface molecules whose functions remain poorly understood. The LAR subfamily of RPTPs has been implicated in axon guidance and neural development. Here we report the molecular and genetic analysis of the C. elegans LAR subfamily member PTP-3. PTP-3 isoforms are expressed in many tissues in early embryogenesis, and later become localized to neuronal processes and to epithelial adherens junctions. Loss of function in ptp-3 causes low-penetrance defects in gastrulation and epidermal development similar to those of VAB-1 Eph receptor tyrosine kinase mutants. Loss of function in ptp-3 synergistically enhances phenotypes of mutations in the C. elegans Eph receptor VAB-1 and a subset of its ephrin ligands, but does not show specific interactions with several other RTKs or morphogenetic mutants. The genetic interaction of vab-1 and ptp-3 suggests that LAR-like RPTPs and Eph receptors have related and partly redundant functions in C. elegans morphogenesis.

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Title: The C. elegans LAR-like receptor tyrosine phosphatase PTP-3 and the VAB-1 Eph receptor tyrosine kinase have partly redundant functions in morphogenesis
Creators: Robert J Harrington - Department of Molecular, Cell, and Developmental Biology, Sinsheimer Laboratories, University of California, Santa Cruz, CA 95064, USA
Michael J Gutch
Michael O Hengartner
Nicholas K Tonks
Andrew D Chisholm
Publication Details: Development (Cambridge), Vol.129(9), pp.2141-2153
Publisher: England
Grant note: R01 GM054657 / NIGMS NIH HHS GM54657 / NIGMS NIH HHS GM55989 / NIGMS NIH HHS
Identifiers: 99900548081901842
Language: English
Resource Type: Journal article