| Mycobacterium tuberculosis PE_PGRS20 and PE_PGRS47 Proteins Inhibit Autophagy by Interaction with Rab1A. | Mycobacterium tuberculosis PE_PGRS20 and PE_PGRS47 Proteins Inhibit Autophagy by Interaction with Rab1A.
Strong EJ, Ng TW, Porcelli SA, Lee S., Free PMC Article | 01/15/2022 |
| Knockdown of Rab1A protein represses proliferation and promotes apoptosis in gastric cancer cells by inhibition of the mTOR/p70S6K pathway. | Rab1A knockdown represses proliferation and promotes apoptosis in gastric cancer cells by inhibition of mTOR/p70S6K pathway.
Li Z, Li Y, Jia Y, Ding B, Yu J. | 07/18/2020 |
| this study shows that Rab1 is required for NLRP3 inflammasome activation and inflammatory lung injury | The GTPase Rab1 Is Required for NLRP3 Inflammasome Activation and Inflammatory Lung Injury.
Zhang Y, Wang L, Lv Y, Jiang C, Wu G, Dull RO, Minshall RD, Malik AB, Hu G., Free PMC Article | 11/9/2019 |
| clear effect of subcutaneous zoledronic acid administration in vivo on the prenylation of Rab1A, Rab5B, Rab7A and Rab14 in mouse peritoneal macrophages, confirming that systemic treatment with bisphosphonate drug can inhibit prenylation in myeloid cells in vivo outside the skeleton. | A highly sensitive prenylation assay reveals in vivo effects of bisphosphonate drug on the Rab prenylome of macrophages outside the skeleton.
Ali N, Jurczyluk J, Shay G, Tnimov Z, Alexandrov K, Munoz MA, Skinner OP, Pavlos NJ, Rogers MJ., Free PMC Article | 01/20/2018 |
| Rab1A regulates anterograde melanosome transport by recruiting kinesin-1 to melanosomes through interaction with SKIP | Rab1A regulates anterograde melanosome transport by recruiting kinesin-1 to melanosomes through interaction with SKIP.
Ishida M, Ohbayashi N, Fukuda M., Free PMC Article | 11/28/2015 |
| These data indicate that AMPylation of Rab1 is an effective strategy to maintain this GTPase on the Legionella-containing vacuole membrane. | AMPylation is critical for Rab1 localization to vacuoles containing Legionella pneumophila.
Hardiman CA, Roy CR., Free PMC Article | 08/30/2014 |
| Rab1A is the first crucial component of the anterograde melanosome transport machinery to be identified in mammalian skin melanocytes. | Functional involvement of Rab1A in microtubule-dependent anterograde melanosome transport in melanocytes.
Ishida M, Ohbayashi N, Maruta Y, Ebata Y, Fukuda M. | 06/15/2013 |
| Acute expression of Rab1 and Rab3d DN constructs partially alleviated this negative feedback mechanism and resulted in impaired ER to Golgi trafficking of procollagen. | Rab GTPase mediated procollagen trafficking in ascorbic acid stimulated osteoblasts.
Nabavi N, Pustylnik S, Harrison RE., Free PMC Article | 04/13/2013 |
| Legionella pneumophila SidD catalyzed AMP release from Rab1, generating de-AMPylated Rab1 accessible for inactivation by LepB; identified SidD as missing link connecting processes of early Rab1 accumulation and subsequent removal during infection | De-AMPylation of the small GTPase Rab1 by the pathogen Legionella pneumophila.
Neunuebel MR, Chen Y, Gaspar AH, Backlund PS Jr, Yergey A, Machner MP., Free PMC Article | 08/6/2011 |
| Results suggest a novel function for Rab1a in the regulation of cell migration through controlling integrin beta1 recycling and localization to lipid rafts via a specific downstream effector pathway. | Regulation of Integrin β 1 recycling to lipid rafts by Rab1a to promote cell migration.
Wang C, Yoo Y, Fan H, Kim E, Guan KL, Guan JL., Free PMC Article | 10/4/2010 |
| Rab1 and Rab6 GTPases may play a role in modulating the function of retina by mediating the transport of nascent proteins along the early secretary pathway, particularly in the process of the light adaptation. | Cell type-specific and light-dependent expression of Rab1 and Rab6 GTPases in mammalian retinas.
Huang W, Wu G, Wang GY., Free PMC Article | 05/10/2010 |
| Data show Trs130 (mTrs130) is a component of an analogous TRAPP complex that this complex is enriched on COPI (Coat Protein I)-coated vesicles it specifically activates Rab1. | mTrs130 is a component of a mammalian TRAPPII complex, a Rab1 GEF that binds to COPI-coated vesicles.
Yamasaki A, Menon S, Yu S, Barrowman J, Meerloo T, Oorschot V, Klumperman J, Satoh A, Ferro-Novick S., Free PMC Article | 02/15/2010 |
| elevated expression of Rab1 protected against alpha-Synuclein-induced dopaminergic neuron loss in animal models of Parkinson Disease | Alpha-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson's models.
Cooper AA, Gitler AD, Cashikar A, Haynes CM, Hill KJ, Bhullar B, Liu K, Xu K, Strathearn KE, Liu F, Cao S, Caldwell KA, Caldwell GA, Marsischky G, Kolodner RD, Labaer J, Rochet JC, Bonini NM, Lindquist S., Free PMC Article | 01/21/2010 |