TheC. elegansLAR-like receptor tyrosine phosphatase PTP-3 and the VAB-1 Eph receptor tyrosine kinase have partly redundant functions in morphogenesis

• DOI: 10.1242/dev.129.9.2141
• Publication Date: 2021-04-26T05:05:29Z
• Authors: Robert J. Harrington; Michael J. Gutch; Michael O. Hengar...; Nicholas K. Tonks; Andrew D. Chisholm
• Keywords: 0301 basic medicine; Cell Cycle Proteins - physiology; Sequence Homology; Cell Cycle Proteins; Protein Tyrosine Phosphatase, Non-Receptor Type 11; Cell Cycle Proteins - genetics; Messenger - genetics; 1309 Developmental Biology; Animals, Genetically Modified; Morphogenesis; Developmental; Cloning, Molecular; Genes, Helminth; Protein Tyrosine Phosphatases - genetics; Protein Tyrosine Phosphatases - physiology; Intracellular Signaling Peptides and Proteins; Protein Tyrosine Phosphatases - chemistry; Gene Expression Regulation, Developmental; Helminth Proteins; 10124 Institute of Molecular Life Sciences; Amino Acid; Caenorhabditis elegans - genetics; Phenotype; Ephrins; 570; Evolution; Molecular Sequence Data; Helminth - genetics; 610; Genetically Modified; Non-Receptor Type 11; Evolution, Molecular; 03 medical and health sciences; Helminth; 1312 Molecular Biology; Animals; Amino Acid Sequence; Caenorhabditis elegans; Caenorhabditis elegans Proteins; Caenorhabditis elegans - growth & development; Helminth Proteins - physiology; Base Sequence; Messenger - metabolism; Molecular; Receptor Protein-Tyrosine Kinases; Caenorhabditis elegans - enzymology; Helminth Proteins - genetics; Genes; Gene Expression Regulation; Mutation; RNA; 570 Life sciences; biology; Protein Tyrosine Phosphatase; Helminth - metabolism; Protein Tyrosine Phosphatases; Cloning

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.