Title : Protein kinase A-dependent phosphorylation of Rap1 regulates its membrane localization and cell migration.

Pub. Date : 2013 Sep 27

PMID : 23946483






7 Functional Relationships(s)
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1 One, it decreases the level of Rap1 activity as measured by GTP loading and the coupling of Rap1 to RapL, a Rap1 effector that couples Rap1 GTP loading to integrin activation. Guanosine Triphosphate RAP1A, member of RAS oncogene family Homo sapiens
2 One, it decreases the level of Rap1 activity as measured by GTP loading and the coupling of Rap1 to RapL, a Rap1 effector that couples Rap1 GTP loading to integrin activation. Guanosine Triphosphate RAP1A, member of RAS oncogene family Homo sapiens
3 One, it decreases the level of Rap1 activity as measured by GTP loading and the coupling of Rap1 to RapL, a Rap1 effector that couples Rap1 GTP loading to integrin activation. Guanosine Triphosphate RAP1A, member of RAS oncogene family Homo sapiens
4 One, it decreases the level of Rap1 activity as measured by GTP loading and the coupling of Rap1 to RapL, a Rap1 effector that couples Rap1 GTP loading to integrin activation. Guanosine Triphosphate RAP1A, member of RAS oncogene family Homo sapiens
5 One, it decreases the level of Rap1 activity as measured by GTP loading and the coupling of Rap1 to RapL, a Rap1 effector that couples Rap1 GTP loading to integrin activation. Guanosine Triphosphate RAP1A, member of RAS oncogene family Homo sapiens
6 These two actions, decreased GTP loading and decreased membrane localization, are related, as the translocation of Rap1-GTP into the cytoplasm is associated with its increased GTP hydrolysis and inactivation. Guanosine Triphosphate RAP1A, member of RAS oncogene family Homo sapiens
7 These two actions, decreased GTP loading and decreased membrane localization, are related, as the translocation of Rap1-GTP into the cytoplasm is associated with its increased GTP hydrolysis and inactivation. Guanosine Triphosphate RAP1A, member of RAS oncogene family Homo sapiens