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Gene Review:

ZFYVE16 - zinc finger, FYVE domain containing 16

Homo sapiens

Synonyms: Endofin, Endosome-associated FYVE domain protein, KIAA0305, PPP1R69, Zinc finger FYVE domain-containing protein 16

Seet, L.F. et al., Chen, Y.G. et al., Seet, L.F. et al., Shi, W. et al., Seet, L.F. et al.

Seet, Liu, Hanson, Hong, Chen, Wang, Ma, Zhang, Lu,

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High impact information on ZFYVE16

In this study, we report that endofin functions as a scaffold protein to facilitate TGF-beta signaling [1].
We further showed that endofin could interact with Smad4 and TGF-beta type I receptors [1].
Knockdown of endogenous endofin expression by RNA interference specifically led to reduction of the transcriptional responses of TGF-beta, but had no effect on BMP- or Wnt1-induced reporter expression [1].
Endofin, a FYVE Domain Protein, Interacts with Smad4 and Facilitates Transforming Growth Factor-beta Signaling [1].
Glutathione S-transferase pull-down assays as well as co-immunoprecipitation experiments confirmed that the carboxyl-terminal half of endofin binds specifically to the carboxyl-terminal region of TOM1 [2].

Biological context of ZFYVE16

To determine its potential effectors or binding partners, we used the carboxyl-terminal half of endofin as bait to screen a human brain cDNA library in a yeast two-hybrid system [2].
Endofin, an endosomal FYVE domain protein [3].
Silencing of endofin by RNAi resulted in a reduction in BMP-dependent Smad1 phosphorylation [4].

Anatomical context of ZFYVE16

The association of endofin with endosomes is mediated by its FYVE domain because deletion mutants lacking the central FYVE finger motif are distributed in the cytoplasm [3].

Associations of ZFYVE16 with chemical compounds

Using in vitro liposome binding assays, we demonstrate that Myc-tagged endofin associates preferentially with phosphatidylinositol 3-phosphate, whereas the C753S point mutant was unable to do so [3].

Co-localisations of ZFYVE16

We also show that endofin co-localizes with SARA but that they are not associated in a common complex because they failed to co-immunoprecipitate in co-expressing cells [3].

Other interactions of ZFYVE16

Taken together, this report provides evidence to suggest that endofin and the highly related SARA are endosomal proteins with potential roles in regulating membrane traffic [3].
Endofin also does not associate with Smad2 nor behave like SARA in affecting transforming growth factor-beta signaling [3].
Endofin recruits clathrin to early endosomes via TOM1 [5].
Taken together, our results suggest that endofin plays an important role in both positive and negative feedback regulation of the BMP signaling pathway [4].

Analytical, diagnostic and therapeutic context of ZFYVE16

Indirect immunofluorescence microscopy using polyclonal antibodies raised against KIAA0305 revealed that it is enriched in early endosomes [3].

References

Endofin, a FYVE Domain Protein, Interacts with Smad4 and Facilitates Transforming Growth Factor-beta Signaling. Chen, Y.G., Wang, Z., Ma, J., Zhang, L., Lu, Z. J. Biol. Chem. (2007) [Pubmed]
Endofin recruits TOM1 to endosomes. Seet, L.F., Liu, N., Hanson, B.J., Hong, W. J. Biol. Chem. (2004) [Pubmed]
Endofin, an endosomal FYVE domain protein. Seet, L.F., Hong, W. J. Biol. Chem. (2001) [Pubmed]
Endofin acts as a Smad anchor for receptor activation in BMP signaling. Shi, W., Chang, C., Nie, S., Xie, S., Wan, M., Cao, X. J. Cell. Sci. (2007) [Pubmed]
Endofin recruits clathrin to early endosomes via TOM1. Seet, L.F., Hong, W. J. Cell. Sci. (2005) [Pubmed]

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