ArticlePloS one2011
Oligomerization of ZFYVE27 (Protrudin) is necessary to promote neurite extension.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 22 citations in OpenAlex.
- Neurodevelopmental Implications Underpinning Hereditary Spastic Paraplegia.CNS neuroscience & therapeutics · 2025Review
- Protrudin regulates FAK activation, endothelial cell migration and angiogenesis.Cellular and molecular life sciences : CMLS · 2022Article
- ARL8 Relieves SKIP Autoinhibition to Enable Coupling of Lysosomes to Kinesin-1.Current biology : CB · 2021Article
- Lysosome Function and Dysfunction in Hereditary Spastic Paraplegias.Brain sciences · 2021Review
- PDZD8 interacts with Protrudin and Rab7 at ER-late endosome membrane contact sites associated with mitochondria.Nature communications · 2020Article
- Axonal Endoplasmic Reticulum Dynamics and Its Roles in Neurodegeneration.Frontiers in neuroscience · 2020Review
- Protrudin modulates seizure activity through GABACell death & disease · 2019Article
- Fatty acid synthase cooperates with protrudin to facilitate membrane outgrowth of cellular protrusions.Scientific reports · 2017Article
- Article
- The role of phosphoinositides in synapse function.Molecular neurobiology · 2014Review
- Medical genomics: The intricate path from genetic variant identification to clinical interpretation.Applied & translational genomics · 2014Review
- Protrudin binds atlastins and endoplasmic reticulum-shaping proteins and regulates network formation.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Generation and characterization of yeast two-hybrid cDNA libraries derived from two distinct mouse pluripotent cell types.Molecular biotechnology · 2013Article
- Phosphoinositides differentially regulate protrudin localization through the FYVE domain.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ZFYVE27 (Protrudin) was originally identified as an interacting partner of spastin, which is most frequently mutated in hereditary spastic paraplegia. ZFYVE27 is a novel member of FYVE family, which is implicated in the formation of neurite extensions by promoting directional membrane trafficking in neurons. Now, through a yeast two-hybrid screen, we have identified that ZFYVE27 interacts with itself and the core interaction region resides within the third hydrophobic region (HR3) of the protein. We confirmed the ZFYVE27's self-interaction in the mammalian cells by co-immunoprecipitation and co-localization studies. To decipher the oligomeric nature of ZFYVE27, we performed sucrose gradient centrifugation and showed that ZFYVE27 oligomerizes into dimer/tetramer forms. Sub-cellular fractionation and Triton X-114 membrane phase separation analysis indicated that ZFYVE27 is a peripheral membrane protein. Furthermore, ZFYVE27 also binds to phosphatidylinositol 3-phosphate lipid moiety. Interestingly, cells expressing ZFYVE27(ΔHR3) failed to produce protrusions instead caused swelling of cell soma. When ZFYVE27(ΔHR3) was co-expressed with wild-type ZFYVE27 (ZFYVE27(WT)), it exerted a dominant negative effect on ZFYVE27(WT) as the cells co-expressing both proteins were also unable to induce protrusions and showed cytoplasmic swelling. Altogether, it is evident that a functionally active form of oligomer is crucial for ZFYVE27 ability to promote neurite extensions.
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