ArticlePloS one2012
MLN64 transport to the late endosome is regulated by binding to 14-3-3 via a non-canonical binding site.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 29 citations in OpenAlex.
- Annexin A6 controls multi-organelle contact site formation and endolysosomal positioning, and remodels the STARD3 interactome.iScience · 2026Article
- Activation of mitochondrial TRAP1 stimulates mitochondria-lysosome crosstalk and correction of lysosomal dysfunction.iScience · 2022Article
- Linking Late Endosomal Cholesterol with Cancer Progression and Anticancer Drug Resistance.International journal of molecular sciences · 2022Review
- STARD3: A Prospective Target for Cancer Therapy.Cancers · 2021Review
- Annexin A6 modulates TBC1D15/Rab7/StARD3 axis to control endosomal cholesterol export in NPC1 cells.Cellular and molecular life sciences : CMLS · 2020Article
- 14-3-3 signal adaptor and scaffold proteins mediate GPCR trafficking.Scientific reports · 2019Article
- Lysosome biogenesis in health and disease.Journal of neurochemistry · 2019Review
- STARD3 mediates endoplasmic reticulum-to-endosome cholesterol transport at membrane contact sites.The EMBO journal · 2017Article
- Subcellular Trafficking of Mammalian Lysosomal Proteins: An Extended View.International journal of molecular sciences · 2016Review
- LDL-cholesterol transport to the endoplasmic reticulum: current concepts.Current opinion in lipidology · 2016Review
- Mitochondrial cholesterol: mechanisms of import and effects on mitochondrial function.Journal of bioenergetics and biomembranes · 2016Review
- Obesity-induced down-regulation of the mitochondrial translocator protein (TSPO) impairs placental steroid production.The Journal of clinical endocrinology and metabolism · 2015Article
- Lipid transport between the endoplasmic reticulum and mitochondria.Cold Spring Harbor perspectives in biology · 2013Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
MLN64 is an integral membrane protein localized to the late endosome and plasma membrane that is thought to function as a mediator of cholesterol transport from endosomal membranes to the plasma membrane and/or mitochondria. The protein consists of two distinct domains: an N-terminal membrane-spanning domain that shares homology with the MENTHO protein and a C-terminal steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domain that binds cholesterol. To further characterize the MLN64 protein, full-length and truncated proteins were overexpressed in cells and the effects on MLN64 trafficking and endosomal morphology were observed. To gain insight into MLN64 function, affinity chromatography and mass spectrometric techniques were used to identify potential MLN64 interacting partners. Of the 15 candidate proteins identified, 14-3-3 was chosen for further characterization. We show that MLN64 interacts with 14-3-3 in vitro as well as in vivo and that the strength of the interaction is dependent on the 14-3-3 isoform. Furthermore, blocking the interaction through the use of a 14-3-3 antagonist or MLN64 mutagenesis delays the trafficking of MLN64 to the late endosome and also results in the dispersal of endocytic vesicles to the cell periphery. Taken together, these studies have determined that MLN64 is a novel 14-3-3 binding protein and indicate that 14-3-3 plays a role in the endosomal trafficking of MLN64. Furthermore, these studies suggest that 14-3-3 may be the link by which MLN64 exerts its effects on the actin-mediated endosome dynamics.
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