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Gene: W02B9.1   

W02B9.1SMapS_parentSequenceSUPERLINK_CB_IR
ChromosomeI
Identity (5)
Gene_info Gene_classhmr
Allele (8)
StrainJJ1079
GO_term (8)
Structured_description Provisional_description hmr-1 encodes two isoforms of a classical cadherin that contain extracellular cadherin, EGF-like, and laminin G domains as well as a highly conserved intracellular domain that binds beta-catenin; by homology, the HMR-1 proteins are predicted to function as calcium-dependent, homophilic cell-cell adhesion receptors; in vivo, HMR-1A activity is required for mediating the cell migrations, cell shape changes, and presumably actin cytoskeleton rearrangements that occur during embryonic morphogenesis; HMR-1B is required for fasciculation and outgrowth of a subset of motor neuron processes; HMR-1 antibodies detect expression in all embryonic blastomeres at early stages of development but as hypodermal adherens junctions form and morphogenesis begins, HMR-1 becomes highly expressed in the apical junctions of all hypodermal cells; later, HMR-1 is expressed primarily at the apical margins of hypodermal, pharyngeal, and intestinal cells in a pattern consistent with localization to adherens junctions; an HMR-1B reporter fusion is expressed in neurons, including the DD, VD, and AS class of motor neurons; HMR-1 activity is required for proper localization of other junctional components, such as HMP-1/alpha-catenin and HMP-2/beta-catenin, but not for localization of AJM-1, the junctional component recognized by the MH27 antibody. Paper_evidence WBPaper00003046
WBPaper00005031
WBPaper00013424
Curator_confirmedWBPerson1843
Date_last_updated24 Jan 2005 00:00:00
hmr-1 encodes two isoforms of a classical cadherin that contain extracellular cadherin, EGF-like, and laminin G domains as well as a highly conserved intracellular domain that binds beta-catenin; by homology, the HMR-1 proteins are predicted to function as a calcium-dependent, homophilic cell-cell adhesion receptor; in vivo, HMR-1A activity is required for mediating the cell migrations, cell shape changes, and presumably actin cytoskeleton rearrangements that occur during embryonic morphogenesis; HMR-1B is required for fasciculation and outgrowth of a subset of motor neuron processes; HMR-1 antibodies detect expression in all embryonic blastomeres at early stages of development but as hypodermal adherens junctions form and morphogenesis begins, HMR-1 becomes highly expressed in the apical junctions of all hypodermal cells; later, HMR-1 is expressed primarily at the apical margins of hypodermal, pharyngeal, and intestinal cells in a pattern consistent with localization to adherens junctions; an HMR-1B reporter fusion is expressed in neurons, including the DD, VD, and AS class of motor neurons; HMR-1 activity is required for proper localization of other junctional components, such as HMP-1/alpha-catenin and HMP-2/beta-catenin, but not for localization of AJM-1, the junctional component recognized by the MH27 antibody. Paper_evidence WBPaper00003046
WBPaper00005031
WBPaper00013424
Person_evidenceWBPerson1843
Concise_description hmr-1 encodes two isoforms of a classical cadherin that contain extracellular cadherin, EGF-like, and laminin G domains as well as a highly conserved intracellular domain that binds beta-catenin; by homology, the HMR-1 proteins are predicted to function as calcium-dependent, homophilic cell-cell adhesion receptors; in vivo, HMR-1A activity is required for mediating the cell migrations, cell shape changes, and presumably actin cytoskeleton rearrangements that occur during embryonic morphogenesis; HMR-1B is required for fasciculation and outgrowth of a subset of motor neuron processes; HMR-1 antibodies detect expression in all embryonic blastomeres at early stages of development but as hypodermal adherens junctions form and morphogenesis begins, HMR-1 becomes highly expressed in the apical junctions of all hypodermal cells; later, HMR-1 is expressed primarily at the apical margins of hypodermal, pharyngeal, and intestinal cells in a pattern consistent with localization to adherens junctions; an HMR-1B reporter fusion is expressed in neurons, including the DD, VD, and AS class of motor neurons; HMR-1 activity is required for proper localization of other junctional components, such as HMP-1/alpha-catenin and HMP-2/beta-catenin, but not for localization of AJM-1, the junctional component recognized by the MH27 antibody.
hmr-1 encodes two isoforms of a classical cadherin that contain extracellular cadherin, EGF-like, and laminin G domains as well as a highly conserved intracellular domain that binds beta-catenin; by homology, the HMR-1 proteins are predicted to function as a calcium-dependent, homophilic cell-cell adhesion receptor; in vivo, HMR-1A activity is required for mediating the cell migrations, cell shape changes, and presumably actin cytoskeleton rearrangements that occur during embryonic morphogenesis; HMR-1B is required for fasciculation and outgrowth of a subset of motor neuron processes; HMR-1 antibodies detect expression in all embryonic blastomeres at early stages of development but as hypodermal adherens junctions form and morphogenesis begins, HMR-1 becomes highly expressed in the apical junctions of all hypodermal cells; later, HMR-1 is expressed primarily at the apical margins of hypodermal, pharyngeal, and intestinal cells in a pattern consistent with localization to adherens junctions; an HMR-1B reporter fusion is expressed in neurons, including the DD, VD, and AS class of motor neurons; HMR-1 activity is required for proper localization of other junctional components, such as HMP-1/alpha-catenin and HMP-2/beta-catenin, but not for localization of AJM-1, the junctional component recognized by the MH27 antibody.
Molecular_info (6)
Experimental_info RNAi_result (8)
WB_RNAi_result (9)
Expr_pattern Expr1435
Expr1788
Interaction WBInteraction0003379
WBInteraction0003380
Reference (41)
RemarkMap position created from combination of previous interpolated map position (based on known location of sequence) and allele information. Therefore this is not a genetic map position based on recombination frequencies or genetic experiments. This was done on advice of the CGC.CGC_data_submission
MethodGene