CELE_F02A9.6, emb-33, F02A9.6

glp-1 encodes an N-glycosylated transmembrane protein that, along with LIN-12, comprises one of two C. elegans members of the LIN-12/Notch family of receptors; from the N- to the C-terminus, GLP-1 is characterized by ten extracellular EGF-like repeats, three LIN-12/Notch repeats, a CC-linker, a transmembrane domain, a RAM domain, six intracellular ankyrin repeats, and a PEST sequence; in C. elegans, GLP-1 activity is required for cell fate specification in germline and somatic tissues; in the germline, GLP-1, acting as a receptor for the DSL family ligand LAG-2, is essential for mitotic proliferation of germ cells and maintenance of germline stem cells; in somatic tissues, maternally provided GLP-1, acting as a receptor for the DSL family ligand APX-1, is required for inductive interactions that specify the fates of certain embryonic blastomeres; GLP-1 is also required for some later embryonic cell fate decisions, and in these decisions its activity is functionally redundant with that of LIN-12; GLP-1 expression is regulated temporally and spatially via translational control, as GLP-1 mRNA, present ubiquitously in the germline and embryo, yields detectable protein solely in lateral, interior, and endomembranes of distal, mitotic germ cells, and then predominantly in the AB blastomere and its descendants in the early embryo; proper spatial translation of glp-1 mRNA in the embryo is dependent upon genes such as the par genes, that are required for normal anterior-posterior asymmetry in the early embryo; signaling through GLP-1 controls the activity of the downstream Notch pathway components LAG-3 and LAG-1, the latter being predicted to function as part of a transcriptional feedback mechanism that positively regulates GLP-1 expression; signaling through the DNA-binding protein LAG-1 is believed to involve a direct interaction between LAG-1 and the GLP-1 RAM and ankyrin domains

CELE_Y18D10A.5, sgg-1, Y18D10A.5

gsk-3 encodes the C. elegans glycogen synthase kinase ortholog; during embryonic development, GSK-3 functions in the Wnt signaling pathway that restricts specification of mesendodermal tissue to the appropriate blastomere; GSK-3 also functions in a Wnt pathway that regulates anteroposterior axon guidance; GSK-3 plays a role in regulating the oocyte-to-embryo transition, by phosphorylating and negatively regulating the OMA-1 zinc finger protein, and in regulation of the oxidative stress response pathway by phosphorylating SKN-1, thereby excluding it from intestinal nuclei; GSK-3, along with MOM-5/Frizzled and APR-1/APC is also required for distal tip cell migration in the gonad and for the engulfment of apoptotic cells, indicating that the Wnt pathway signals to CED-10/Rac to regulate cytoskeletal rearrangement during different cellular processes; GSK-3 can be phosphorylated by murine ERK2 in vitro, suggesting that it is a substrate for the RTK-RAS-ERK pathway in vivo; consistent with this, GSK-3 phosphorylation is absent in mpk-1 mutant animals.