GRAB is a binding partner for the Rab11a and Rab11b GTPases

Horgan, Conor P.; Hanscom, Sara R.; McCaffrey, Mary W.

doi:10.1016/j.bbrc.2013.10.043

Cited by 20 publications

(23 citation statements)

References 34 publications

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“…We examined the specificity of the increase in Rab7 activity on maturing macropinosomes by a similar time-lapse experiment using Raichu-Rab7-NC as a negative control sensor, because the dominant-negative form, Racihu-Rab7-T22N, inhibits macropinosome formation and thus cannot be used. In Raichu-Rab7-NC, the Rab7-binding domain of Rabring7 was replaced with the Rab11-binding domain of GRAB (also known as RAB3IL1) (Horgan et al, 2013). Validation of this negative control was shown by the fact that the expression of Armus-GAP did not decrease the FRET/CFP ratio of RacihuRab7-NC (Fig.…”

Section: Development Of a Sensor For Rab7 Activitymentioning

confidence: 99%

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Mon1-Ccz1 activates Rab7 only on late endosome and dissociates from lysosome in mammalian cells

Yasuda

Morishita

Fujita

et al. 2015

Journal of Cell Science

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Rab GTPases act as molecular switches regulating various aspects of membrane trafficking. Among them, Rab5 and Rab7 play central roles in the endolysosomal network. Although many effectors downstream of Rab7 have been elucidated, our present understanding of the mechanism regulating Rab7 activity is extremely limited. It has only recently been accepted that Mon1-Ccz1 is a Rab7 guanine nucleotide exchange factor, but the question where Mon1-Ccz1 works with Rab7 is hardly answered. To address what kind of change/switch exists in the regulatory mechanism upstream of Rab7 during the transition from late endosome to lysosome, we examined Rab7 activity in steady-state cells and EGF-induced macropinocytosis using a newly developed FRET sensor. A combination of a Rab7 sensor and confocal FRET imaging techniques revealed that the activation of Rab7 on late endosomes depends on Mon1-Ccz1 and is implicated in late endosome-lysosome fusion. In contrast, Rab7 activity on lysosomes was independent of Mon1-Ccz1 and active Rab7 played a role in perinuclear clustering of lysosomes.

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Section: Development Of a Sensor For Rab7 Activitymentioning

confidence: 99%

“…If necessary, wild-type Rab7 was replaced with Rab7-Q67L or Rab7-T22N. In pRaichu-Rab7-NC, the Rab7-binding domain of Rabring7 was replaced with the Rab11-binding domain of GRAB (Horgan et al, 2013).…”

Section: Fret Biosensorsmentioning

confidence: 99%

Mon1-Ccz1 activates Rab7 only on late endosome and dissociates from lysosome in mammalian cells

Yasuda

Morishita

Fujita

et al. 2015

Journal of Cell Science

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“…Ip6k1 (Luo et al, 2001) Rab11 (Horgan et al, 2013) Others SH3BP5 (9467) REI-1 Rab11 (Sakaguchi et al, 2015) 1,3…”

Section: Ishida Et Almentioning

confidence: 99%

Multiple Types of Guanine Nucleotide Exchange Factors (GEFs) for Rab Small GTPases

Ishida

Oguchi

Fukuda

2016

Cell Struct. Funct.

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ABSTRACT. Rab small GTPases are highly conserved master regulators of membrane traffic in all eukaryotes. The same as the activation and inactivation of other small GTPases, the activation and inactivation of Rabs are tightly controlled by specific GEFs (guanine nucleotide exchange factors) and GAPs (GTPase-activating proteins), respectively. Although almost all Rab-GAPs reported thus far have a TBC (Tre-2/Bub2/Cdc16)/Rab-GAP domain in common, recent accumulating evidence has indicated the existence of a number of structurally unrelated types of Rab-GEFs, including DENN proteins, VPS9 proteins, Sec2 proteins, TRAPP complexes, heterodimer GEFs (Mon1-Ccz1, HPS1-HPS4 (BLOC-3 complex), Ric1-Rgp1 and Rab3GAP1/2), and other GEFs (e.g., REI-1 and RPGR). In this review article we provide an up-to-date overview of the structures and functions of all putative Rab-GEFs in mammals, with a special focus on their substrate Rabs, interacting proteins, associations with genetic diseases, and intracellular localizations.

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“…Interestingly, two Rab8 GEFs, the guanine nucleotide exchange factor for Rab3A (GRAB) and Rabin8, are also Rab11 effectors, suggesting a hierarchical regulation of membrane recycling [Horgan et al, 2013;Knodler et al, 2010]. Only in recent years it has become apparent that often two or more Rab GTPases are functionally linked in networks controlling membrane transport [Mizuno-Yamasaki et al, 2012].…”

Section: Rab8mentioning

confidence: 99%

Rab GTPase signaling in neurite outgrowth and axon specification

2016

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Neurons are highly polarized cells that contain specialized subcellular domains involved in information transmission in the nervous system. Specifically, the somatodendritic compartment receives neuronal inputs while the axons convey information through the synapse. The establishment of asymmetric domains requires a specific delivery of components, including organelles, proteins, and membrane. The Rab family of small GTPases plays an essential role in membrane trafficking. Signaling cascades triggered by extrinsic and intrinsic factors tightly regulate Rab functions in cells, with Rab protein activation depending on GDP/GTP binding to establish a binary mode of action. This review summarizes the contributions of several Rab family members involved in trans-Golgi, early/late endosomes, and recycling endosomes during neurite development and axonal outgrowth. The regulation of some Rabs by guanine exchanging factors and GTPase activating proteins will also be addressed. Finally, discussion will be provided on how specific effector-mediated Rab activation modifies several molecules essential to neuronal differentiation. V C 2016 Wiley Periodicals, Inc.

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GRAB is a binding partner for the Rab11a and Rab11b GTPases

Cited by 20 publications

References 34 publications

Mon1-Ccz1 activates Rab7 only on late endosome and dissociates from lysosome in mammalian cells

Mon1-Ccz1 activates Rab7 only on late endosome and dissociates from lysosome in mammalian cells

Multiple Types of Guanine Nucleotide Exchange Factors (GEFs) for Rab Small GTPases

Rab GTPase signaling in neurite outgrowth and axon specification

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