Over-expression of Rififylin, a new RING finger and FYVE-like domain-containing protein, inhibits recycling from the endocytic recycling compartment

Molecular Biology of the Cell
Franck CoumailleauMichel Cohen-Tannoudji

Abstract

Endocytosed membrane components are recycled to the cell surface either directly from early/sorting endosomes or after going through the endocytic recycling compartment (ERC). Studying recycling mechanisms is difficult, in part due to the fact that specific tools to inhibit this process are scarce. In this study, we have characterized a novel widely expressed protein, named Rififylin (Rffl) for RING Finger and FYVE-like domain-containing protein, that, when overexpressed in HeLa cells, induced the condensation of transferrin receptor-, Rab5-, and Rab11-positive recycling tubulovesicular membranes in the perinuclear region. Internalized transferrin was able to access these condensed endosomes but its exit from this compartment was delayed. Using deletion mutants, we show that the carboxy-terminal RING finger of Rffl is dispensable for its action. In contrast, the amino-terminal domain of Rffl, which shows similarities with the phosphatidylinositol-3-phosphate-binding FYVE finger, is critical for the recruitment of Rffl to recycling endocytic membranes and for the inhibition of recycling, albeit in a manner that is independent of PtdIns(3)-kinase activity. Rffl overexpression represents a novel means to inhibit recycling that wil...Continue Reading

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Citations

Feb 21, 2006·Cancer Research·Xing-Jie LiangMichael M Gottesman
Dec 27, 2005·Cell·Laxminarayana R DevireddyMichael R Green
Mar 5, 2005·Médecine sciences : M/S·Franck CoumailleauMichel Cohen-Tannoudji
Apr 9, 2020·Journal of Cell Science·Christian RenzHelle D Ulrich
Feb 6, 2021·Journal of Clinical Medicine·Shipra Agrawal On Behalf Of The Pediatric Nephrology Research Consortium Pnrc

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