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SPG33 protein protrudin contains hydrophobic, intramembrane hairpin domains, interacts with tubular ER proteins, and functions in ER morphogenesis by regulating the sheet-to-tubule balance and possibly the density of tubule interconnections.
findings indicate that protrudin interacts with spastin (zeige SPAST ELISA Kits) and induces axon formation through its N-terminal domain. Moreover, protrudin and spastin (zeige SPAST ELISA Kits) may work together to play an indispensable role in motor axon outg
Protrudin-KIF5 com (zeige KIF5A ELISA Kits)plex contributes to the vesicular trans (zeige KIF5A ELISA Kits)port in neurons.
protrudin regulates Rab11 (zeige RAB11A ELISA Kits)-dependent membrane recycling to promote the directional membrane trafficking required for neurite formation [protrudin]
The role of ZFYVE27/protrudin in hereditary spastic paraplegia is reported.
VAP-A (zeige VAPA ELISA Kits) is an important regulator both of the subcellular localization of protrudin and of its ability to stimulate neurite outgrowth.
We found that Zfyve27, which encodes protrudin, identified a subpopulation of papillary label-retaining cells (pLRCs). With Zfyve27-CreERT2 transgenic and reporter mice we generated bitransgenic animals and performed cell-lineage analysis. Post tamoxifen, Zfyve27-CreERT2 marked cells preferentially located in the upper part of the papilla.
Identification and characterization of protrudin-L, neuron-specific isoform of protrudin that promotes axonal elongation and contributes to the establishment of neuronal polarity.
Phosphoinositides differentially regulate protrudin localization through the FYVE domain [protrudin]
protrudin contributes to the regulation of ER morphology and function, and that its deregulation by mutation is a causative defect in HSP.
Protrudin and KIF5 (zeige KIF5A ELISA Kits) interact in mouse brain.Protrudin-KIF5 (zeige KIF5A ELISA Kits) complex contributes to the vesicular transport in neurons.
This gene encodes a protein with several transmembrane domains, a Rab11-binding domain and a lipid-binding FYVE finger domain. The encoded protein appears to promote neurite formation. A mutation in this gene has been reported to be associated with hereditary spastic paraplegia, however the pathogenicity of the mutation, which may simply represent a polymorphism, is unclear.
zinc finger, FYVE domain containing 27
, zinc finger FYVE domain-containing protein 27
, Zinc finger FYVE domain-containing protein 27