Pericentrosomal targeting of Rab6 secretory vesicles by Bicaudal-D-related protein 1 (BICDR-1) regulates neuritogenesis

Schlager, Max A.; Kapitein, Lukas C.; Grigoriev, Ilya; Burzynski, Grzegorz M.; Wulf, Phebe S.; Keijzer, Nanda; Graaff, Esther de; Fukuda, Mitsunori; Shepherd, Iain T.; Akhmanova, Anna; Hoogenraad, Casper C.

doi:10.1038/emboj.2010.51

Cited by 158 publications

(212 citation statements)

References 48 publications

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“…Tambe et al propose that both PNN/DRS and RAB24 may be involved in the progression of autophagy. Schlager et al 27 have performed a GST affinity isolation assay with GSTimmobilized RAB proteins, and observe that, similar to several other RABs, RAB24 weakly binds CCDC64B/BICDR2 (a putative RAB6 effector). The strongest binding partner of CCDC64B/BICDR2 in this assay was RAB13.…”

Section: Discussionmentioning

confidence: 99%

RAB24 facilitates clearance of autophagic compartments during basal conditions

et al. 2015

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RAB24 belongs to a family of small GTPases and has been implicated to function in autophagy. Here we confirm the intracellular localization of RAB24 to autophagic vacuoles with immuno electron microscopy and cell fractionation, and show that prenylation and guanine nucleotide binding are necessary for the targeting of RAB24 to autophagic compartments. Further, we show that RAB24 plays a role in the maturation and/or clearance of autophagic compartments under nutrient-rich conditions, but not during short amino acid starvation. Quantitative electron microscopy shows an increase in the numbers of late autophagic compartments in cells silenced for RAB24, and mRFP-GFP-LC3 probe and autophagy flux experiments indicate that this is due to a hindrance in their clearance. Formation of autophagosomes is shown to be unaffected by RAB24-silencing with siRNA. A defect in aggregate clearance in the absence of RAB24 is also shown in cells forming polyglutamine aggregates. This study places RAB24 function in the termination of the autophagic process under nutrient-rich conditions.

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Section: Discussionmentioning

confidence: 99%

RAB24 facilitates clearance of autophagic compartments during basal conditions

et al. 2015

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“…Even though axons appear to be narrow tubes, their trafficking system is complicated. Their membrane supplies are derived from endocytic and secretory vesicles, and many Rabs (e.g., Rab6, Rab8, Rab10, Rab11, Rab27, Rab33, and Rab35) are involved (Huber et al, 1995;Arimura et al, 2009;Schlager et al, 2010;Wang et al, 2011;Kobayashi and Fukuda, 2012;Nakazawa et al, 2012;Takano et al, 2012). Rab35 supports Cdc42 activation, an essential feature during axon specification and elongation (Villarroel-Campos et al, 2016b).…”

Section: Discussionmentioning

confidence: 99%

“…The plasmids, pEGFP-Rab8A, pEGFP-Rab11A, their constitutively active (ca) and constitutively inactive (ci)-containing mutants, and pmStr-Rab11A were described previously (Fukuda, 2003;Sano et al, 2008;Mori et al, 2012). pEGFP-GRAB, pmStr-GRAB, and pEF-GRAB were prepared as described previously (Mori et al, 2013).…”

Section: Methodsmentioning

confidence: 99%

Cdk5 Regulation of the GRAB-Mediated Rab8-Rab11 Cascade in Axon Outgrowth

et al. 2017

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Neurons communicate with each other through their axons and dendrites. However, a full characterization of the molecular mechanisms involved in axon and dendrite formation is still incomplete. Neurite outgrowth requires the supply of membrane components for surface expansion. Two membrane sources for axon outgrowth are suggested: Golgi secretary vesicles and endocytic recycling endosomes. In non-neuronal cells, trafficking of secretary vesicles from Golgi is regulated by Rab8, a member of Rab small GTPases, and that of recycling endosomes is by Rab11, another member of Rabs. However, whether these vesicles are coordinately or independently transported in growing axons is unknown. Herein, we find that GRAB, a guanine nucleotide exchange factor for Rab8, is a novel regulator of axon outgrowth. Knockdown of GRAB suppressed axon outgrowth of cultured mouse brain cortical neurons. GRAB mediates the interaction between Rab11A and Rab8A, and this activity is regulated by phosphorylation at Ser169 and Ser180 by Cdk5-p35. The nonphosphorylatable GRAB mutant S169/180A promoted axonal outgrowth to a greater extent than did the phosphomimetic GRAB mutant S169/180D. Phosphorylation of GRAB suppressed its guanine nucleotide exchange factor activity and its ability to recruit Rab8A-to Rab11A-positive endosomes. In vivo function of GRAB and its Cdk5-phophorylation were shown in migration and process formation of developing neurons in embryonic mouse brains. These results indicate that GRAB regulates axonal outgrowth via activation and recruitment of Rab8A-to Rab11A-positive endosomes in a Cdk5-dependent manner.

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“…Moreover, several Rab isoforms, e.g. Rab3A, Rab9, Rab11, and Rab27, indirectly interact with particular kinesins via their effector molecules (Jackson et al, 2008;Niwa et al, 2008;Arimura et al, 2009;Schlager et al, 2010). These observations led us to hypothesize that a certain as yet unidentified Rab isoform is also involved in anterograde melanosome transport in mammalian skin melanocytes.…”

Section: Introductionmentioning

confidence: 99%

Functional involvement of Rab1A in microtubule-dependent anterograde melanosome transport in melanocytes

Ishida

Ohbayashi

Maruta

et al. 2012

Journal of Cell Science

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SummaryMelanosomes are transported to the cell periphery of melanocytes by coordination between bidirectional microtubule-dependent movements and unidirectional actin-dependent movement. Although both the mechanism of the actin-dependent melanosome transport and the mechanism of the microtubule-dependent retrograde melanosome transport in mammalian skin melanocytes have already been determined, almost nothing is known about the mechanism of the microtubule-dependent anterograde melanosome transport. Small GTPase Rab proteins are common regulators of membrane traffic in all eukaryotes, and in this study we performed genome-wide screening for Rab proteins that are involved in anterograde melanosome transport by expressing 60 different constitutive active (and negative) mutants, and succeeded in identifying Rab1A, originally described as a Golgi-resident Rab, as a prime candidate. Endogenous Rab1A protein was found to be localized to mature melanosomes in melanocytes, and its functional ablation either by siRNA-mediated knockdown or by overexpression of a cytosolic form of Rab1A-GTPase-activating protein/TBC1D20 induced perinuclear melanosome aggregation. The results of time-lapse imaging further revealed that long-range anterograde melanosome movements were specifically suppressed in Rab1A-deficient melanocytes, whereas retrograde melanosome transport occurred normally. Taken together, these findings indicate that Rab1A is the first crucial component of the anterograde melanosome transport machinery to be identified in mammalian skin melanocytes.

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Pericentrosomal targeting of Rab6 secretory vesicles by Bicaudal-D-related protein 1 (BICDR-1) regulates neuritogenesis

Cited by 158 publications

References 48 publications

RAB24 facilitates clearance of autophagic compartments during basal conditions

RAB24 facilitates clearance of autophagic compartments during basal conditions

Cdk5 Regulation of the GRAB-Mediated Rab8-Rab11 Cascade in Axon Outgrowth

Functional involvement of Rab1A in microtubule-dependent anterograde melanosome transport in melanocytes

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