NIMA interacting proteins
AssigneeThe Salk Institute for Biological Studies
InventorsTony Hunter, Kun Ping Lu
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Abstract
A novel class of NIMA interacting proteins (PIN), exemplified by Pin1, is provided. Pin1 induces a G2 arrest and delays NIMA-induced mitosis when overexpressed, and triggers mitotic arrest and DNA fragmentation when depleted. Methods of identifying other Pin proteins and Pin-interacting proteins and identifying compositions which affect Pin activity or expression are also provided.
Claims4
A substantially pure WW domain of a Pin1 polypeptide consisting of amino acid residues 5–43 of SEQ ID NO:2, or a functional fragment thereof which binds to NIMA.
A substantially pure PPIase domain of a Pin1 polypeptide consisting of amino acid residues 59–163 of SEQ ID NO:2, or a functional fragment thereof having peptidyl prolyl isomerase activity.
A substantially pure fragment of a Pin1 polypeptide, which Pin1 polypeptide consists of amino acid residue 1–163 of SEQ ID NO:2, wherein the fragment comprises amino acid residues 5–43 of SEQ ID NO:2 and binds to NIMA.
A substantially pure fragment of a Pin1 polypeptide, which Pin1 polypeptide consists of amino acid residue 1–163 of SEQ ID NO:2, wherein the fragment comprises amino acid residues 59–163 of SEQ ID NO:2 and has peptidyl prolyl isomerase activity.
Dependencies are inferred from the claim text.