P4-ATPase endosomal recycling relies on multiple retromer-dependent localization signals.
| Autor: | Jiménez M; Department of Biological Sciences, Vanderbilt University, Nashville, TN 37235., Kyoung CK; Department of Biological Sciences, Vanderbilt University, Nashville, TN 37235., Nabukhotna K; Department of Biological Sciences, Vanderbilt University, Nashville, TN 37235., Watkins D; Department of Biological Sciences, Vanderbilt University, Nashville, TN 37235., Jain BK; Department of Biological Sciences, Vanderbilt University, Nashville, TN 37235., Best JT; Department of Biological Sciences, Vanderbilt University, Nashville, TN 37235., Graham TR; Department of Biological Sciences, Vanderbilt University, Nashville, TN 37235. |
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| Jazyk: | angličtina |
| Zdroj: | Molecular biology of the cell [Mol Biol Cell] 2024 Oct 01; Vol. 35 (10), pp. ar125. Date of Electronic Publication: 2024 Aug 07. |
| DOI: | 10.1091/mbc.E24-05-0209 |
| Abstrakt: | Type IV P-type ATPases (P4-ATPases) are lipid flippases that generate an asymmetric membrane organization essential for cell viability. The five budding yeast P4-ATPases traffic between the Golgi complex, plasma membrane, and endosomes but how they are recycled from the endolysosomal system to the Golgi complex is poorly understood. In this study, we find that P4-ATPase endosomal recycling is primarily driven by the retromer complex and the F-box protein Rcy1. Defects in P4-ATPase recycling result in their mislocalization to the vacuole and a substantial loss of membrane asymmetry. The P4-ATPases contain multiple predicted retromer sorting signals, and the characterization of these signals in Dnf1 and Dnf2 led to the identification of a novel retromer-dependent signal, IPM[ST] that acts redundantly with predicted motifs. Together, these results emphasize the importance of endosomal recycling for the functional localization of P4-ATPases and membrane organization. Competing Interests: Conflicts of interest: The authors declare no financial conflict of interest. |
| Databáze: | MEDLINE |
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