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Gene Review:

GULP1 - GULP, engulfment adaptor PTB domain...

Homo sapiens

Synonyms: CED-6, CED6, Cell death protein 6 homolog, GULP, PTB domain adapter protein CED-6, ...

Su, H.P. et al., Liu, Q.A. et al., Smits, E. et al., Ranganathan, S. et al.

Smits, Van Criekinge, Plaetinck, Bogaert,

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High impact information on GULP1

Furthermore, serine and threonine phosphorylation increased the interaction of LRP with other adaptor proteins such as Dab-1 and CED-6/GULP [1].
Identification and characterization of a dimerization domain in CED-6, an adapter protein involved in engulfment of apoptotic cells [2].
In this report, we demonstrate that CED-6 dimerizes through a leucine zipper domain that is immediately adjacent to the PTB domain [2].
CED-6 is composed of a phosphotyrosine-binding (PTB) domain and a proline-rich C-terminal domain with no apparent catalytic domain [2].
The human homologue of Caenorhabditis elegans CED-6 specifically promotes phagocytosis of apoptotic cells [3].

Biological context of GULP1

As is the case with the worm protein, hCED-6 contains a phosphotyrosine-binding (PTB) domain and potential Src-homology domain 3 (SH3) binding sites [4].
Thus, CED-6, and the CED-6 signal transduction pathway, might be conserved from C. elegans to humans and are present in most, if not all, human tissues [4].

Anatomical context of GULP1

The 34 kDa hCED-6 protein is expressed in most tissues, some human cancer cells, and in primary human macrophages [3].

Analytical, diagnostic and therapeutic context of GULP1

Several lines of evidence based on co-immunoprecipitation studies, yeast two-hybrid assays, and gel filtration studies suggest that CED-6 exists as a dimer in vivo [2].

References

Serine and threonine phosphorylation of the low density lipoprotein receptor-related protein by protein kinase Calpha regulates endocytosis and association with adaptor molecules. Ranganathan, S., Liu, C.X., Migliorini, M.M., Von Arnim, C.A., Peltan, I.D., Mikhailenko, I., Hyman, B.T., Strickland, D.K. J. Biol. Chem. (2004) [Pubmed]
Identification and characterization of a dimerization domain in CED-6, an adapter protein involved in engulfment of apoptotic cells. Su, H.P., Brugnera, E., Van Criekinge, W., Smits, E., Hengartner, M., Bogaert, T., Ravichandran, K.S. J. Biol. Chem. (2000) [Pubmed]
The human homologue of Caenorhabditis elegans CED-6 specifically promotes phagocytosis of apoptotic cells. Smits, E., Van Criekinge, W., Plaetinck, G., Bogaert, T. Curr. Biol. (1999) [Pubmed]
Human CED-6 encodes a functional homologue of the Caenorhabditis elegans engulfment protein CED-6. Liu, Q.A., Hengartner, M.O. Curr. Biol. (1999) [Pubmed]

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ced-6	Caenorhabditis elegans
gulp1a	Danio rerio
LOC708601	Macaca mulatta
Gulp1	Mus musculus
GULP1	Pan troglodytes
Gulp1	Rattus norvegicus

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