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Extracellular proteins needed for C. elegans mechanosensation. Export

Neuron, Vol. 16 (1996), pp. 183-194.

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amino_acid_sequence article base_sequence c50h23 caenorhabditis_elegans caenorhabditis_elegans_genetics caenorhabditis_elegans_physiology celegans c_elegans collagen_genetics collagen_physiology e03g23 elegans epistasis_genetic extracellular_matrix_physiology extracellular_matrix_proteins_chemistry extracellular_matrix_proteins_genetics extracellular_matrix_proteins_physiology f01d46 fluorescent_dyes genes_recessive genes_reporter genes_structural_helminth helminth_proteins_chemistry helminth_proteins_genetics helminth_proteins_physiology mec-3 mec-5 mec-9 mechanoreceptors_physiology molecular_sequence_data mutagenesis_site_directed nematode neurons_afferent_chemistry neurons_afferent_physiology protein_structure_tertiary recombinant_fusion_proteins_analysis repetitive_sequences_nucleic_acid sequence_alignment sequence_homology_amino_acid touch_physiology wormbase

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The mec-5 and mec-9 genes encode putative extracellular proteins that allow a set of six touch receptor neurons in C. elegans to respond to gentle touch. MEC-5 is a collagen made by the epidermal cells that surround the touch cells. Mutations causing touch insensitivity affect the Gly-X-Y repeats of this collagen. mec-9 produces two transcripts, the larger of which is expressed in the touch cells and two PVD neurons. This transcript encodes a protein with 5 Kunitz-type protease inhibitor domains, 6 EGF-like repeats (2 of the Ca2+-binding type), and a glutamic acid-rich region. Missense mutations causing touch insensitivity affect both the EGF-like and Kunitz domains. Since mec-9 loss of function mutations dominantly enhance the touch insensitive phenotype of several mec-5 mutations, MEC-5 and MEC-9 may interact. We propose that these proteins provide an extracellular attachment point for the mechanosensory channels of the touch cells.


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