PMID:9857183

Citation	Izumi, Y, Hirata, M, Hasuwa, H, Iwamoto, R, Umata, T, Miyado, K, Tamai, Y, Kurisaki, T, Sehara-Fujisawa, A, Ohno, S and Mekada, E (1998) A metalloprotease-disintegrin, MDC9/meltrin-gamma/ADAM9 and PKCdelta are involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor. EMBO J. 17:7260-72
Abstract	The ectodomains of many proteins located at the cell surface are shed upon cell stimulation. One such protein is the heparin-binding EGF-like growth factor (HB-EGF) that exists in a membrane-anchored form which is converted to a soluble form upon cell stimulation with TPA, an activator of protein kinase C (PKC). We show that PKCdelta binds in vivo and in vitro to the cytoplasmic domain of MDC9/meltrin-gamma/ADAM9, a member of the metalloprotease-disintegrin family. Furthermore, the presence of constitutively active PKCdelta or MDC9 results in the shedding of the ectodomain of proHB-EGF, whereas MDC9 mutants lacking the metalloprotease domain, as well as kinase-negative PKCdelta, suppress the TPA-induced shedding of the ectodomain. These results suggest that MDC9 and PKCdelta are involved in the stimulus-coupled shedding of the proHB-EGF ectodomain.
Links	PubMed PMC1171072 Online version:10.1093/emboj/17.24.7260
Keywords	ADAM Proteins; Catalytic Domain/genetics; Disintegrins/genetics; Disintegrins/metabolism; Epidermal Growth Factor/metabolism; Intercellular Signaling Peptides and Proteins; Isoenzymes/metabolism; Membrane Proteins/genetics; Membrane Proteins/metabolism; Metalloendopeptidases/metabolism; Muscle Proteins/metabolism; Mutation; Protein Binding; Protein Kinase C/metabolism; Protein Kinase C-delta; Protein Precursors/metabolism; Protein Processing, Post-Translational; Recombinant Proteins/metabolism; Solubility; Tetradecanoylphorbol Acetate/pharmacology
edit table

Annotations

Gene product	Qualifier	GO ID	GO term name	Evidence Code	with/from	Aspect	Notes	Status
edit table

References

See Help:References for how to manage references in GONUTS.