Protrudin-mediated ER-endosome contact sites promote MT1-MMP exocytosis and cell invasion. | Protrudin-mediated ER-endosome contact sites promote MT1-MMP exocytosis and cell invasion. Pedersen NM, Wenzel EM, Wang L, Antoine S, Chavrier P, Stenmark H, Raiborg C., Free PMC Article | 03/27/2021 |
Protrudin functions from the endoplasmic reticulum to support axon regeneration in the adult CNS. | Protrudin functions from the endoplasmic reticulum to support axon regeneration in the adult CNS. Petrova V, Pearson CS, Ching J, Tribble JR, Solano AG, Yang Y, Love FM, Watt RJ, Osborne A, Reid E, Williams PA, Martin KR, Geller HM, Eva R, Fawcett JW., Free PMC Article | 12/5/2020 |
Protrudin and PDZD8 contribute to neuronal integrity by promoting lipid extraction required for endosome maturation. | Protrudin and PDZD8 contribute to neuronal integrity by promoting lipid extraction required for endosome maturation. Shirane M, Wada M, Morita K, Hayashi N, Kunimatsu R, Matsumoto Y, Matsuzaki F, Nakatsumi H, Ohta K, Tamura Y, Nakayama KI., Free PMC Article | 10/3/2020 |
Protrudin modulates seizure activity through GABAA receptor regulation. | Protrudin modulates seizure activity through GABA(A) receptor regulation. Lu X, Yang Y, Zhou R, Li Y, Yang Y, Wang X., Free PMC Article | 09/5/2020 |
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. | Protrudin binds atlastins and endoplasmic reticulum-shaping proteins and regulates network formation. Chang J, Lee S, Blackstone C., Free PMC Article | 12/14/2013 |
findings indicate that protrudin interacts with spastin and induces axon formation through its N-terminal domain. Moreover, protrudin and spastin may work together to play an indispensable role in motor axon outg | Role of spastin and protrudin in neurite outgrowth. Zhang C, Li D, Ma Y, Yan J, Yang B, Li P, Yu A, Lu C, Ma X. | 11/3/2012 |
Protrudin-KIF5 complex contributes to the vesicular transport in neurons. | Protrudin serves as an adaptor molecule that connects KIF5 and its cargoes in vesicular transport during process formation. Matsuzaki F, Shirane M, Matsumoto M, Nakayama KI., Free PMC Article | 04/14/2012 |
Observational study of gene-disease association. (HuGE Navigator) | A scan of chromosome 10 identifies a novel locus showing strong association with late-onset Alzheimer disease. Grupe A, Li Y, Rowland C, Nowotny P, Hinrichs AL, Smemo S, Kauwe JS, Maxwell TJ, Cherny S, Doil L, Tacey K, van Luchene R, Myers A, Wavrant-De Vrièze F, Kaleem M, Hollingworth P, Jehu L, Foy C, Archer N, Hamilton G, Holmans P, Morris CM, Catanese J, Sninsky J, White TJ, Powell J, Hardy J, O'Donovan M, Lovestone S, Jones L, Morris JC, Thal L, Owen M, Williams J, Goate A., Free PMC Article | 12/2/2009 |
VAP-A is an important regulator both of the subcellular localization of protrudin and of its ability to stimulate neurite outgrowth. | Promotion of neurite extension by protrudin requires its interaction with vesicle-associated membrane protein-associated protein. Saita S, Shirane M, Natume T, Iemura SI, Nakayama KI., Free PMC Article | 01/21/2010 |
The role of ZFYVE27/protrudin in hereditary spastic paraplegia is reported. | The role of ZFYVE27/protrudin in hereditary spastic paraplegia. Martignoni M, Riano E, Rugarli EI., Free PMC Article | 01/21/2010 |
protrudin regulates Rab11-dependent membrane recycling to promote the directional membrane trafficking required for neurite formation [protrudin] | Protrudin induces neurite formation by directional membrane trafficking. Shirane M, Nakayama KI. | 01/21/2010 |
Mutation affects neuronal intracellular trafficking in the corticospinal tract, which is consistent with the pathology of hereditary spastic paraplegia. | ZFYVE27 (SPG33), a novel spastin-binding protein, is mutated in hereditary spastic paraplegia. Mannan AU, Krawen P, Sauter SM, Boehm J, Chronowska A, Paulus W, Neesen J, Engel W., Free PMC Article | 01/21/2010 |