Diverse roles of the scaffolding protein RanBPM

Suresh, Bharathi; Ramakrishna, Suresh; Baek, Kwang‐Hyun

doi:10.1016/j.drudis.2011.10.030

Cited by 38 publications

(47 citation statements)

References 67 publications

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“…The existence of both RanBP9 and COPS5 in the same protein complexes suggests that they may interact with each other and that such an interaction has functional significance. RanBP9 is a multimodular scaffold protein known to interact with a great variety of proteins in almost every subcellular compartment in the cell, including the plasma membrane (8). Like RanBP9 (20 -22) COPS5 is also present in the cytoplasm, nucleus, and at the inner leaflet of the plasma membrane, especially when it is in the free form but not when bound to the COP9 signalosome (16,23,24), suggesting that both proteins might interact at more than one subcellular location.…”

Section: Discussionmentioning

confidence: 99%

“…The versatile nature of RanBP9 interaction with diverse proteins is believed to result in several multiprotein complexes involved in regulating many signaling pathways. The domain organization of RanBP9 includes the proline-rich domain, PRY, SPRY (SPla and the ryanodine receptor), LisH, and CTLH, which are all protein-protein binding domains that greatly increase the number of possible interactions of a wide variety of proteins with RanBP9 (8,11), making it a perfect protein for scaffolding function. Our two-hybrid screen and domain-mapping experiments suggest that it is the LisH domain of RanBP9 that specifically interacts with COPS5.…”

Section: Discussionmentioning

confidence: 99%

“…RanBP9 is a scaffolding protein implicated in a variety of functions through integration of cell surface receptors with intracellular signaling targets (8). Recently, RanBP9 was found to be within the clusters of RNA transcript pairs associated with markers of AD progression, suggesting that RanBP9 might contribute to the pathogenesis of AD (9).…”

Section: Alzheimer's Disease (Ad)mentioning

confidence: 99%

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COPS5 (Jab1) Protein Increases β Site Processing of Amyloid Precursor Protein and Amyloid β Peptide Generation by Stabilizing RanBP9 Protein Levels

Wang

Dey

Carrera

et al. 2013

Journal of Biological Chemistry

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Background: Increased generation of toxic amyloid ␤ peptide (A␤) in the brain is central to the pathogenesis of Alzheimer's disease (AD). Results: COPS5 (Jab1) is a novel RanBP9-interacting protein that robustly increases A␤ generation Conclusion: COPS5 increases A␤ generation by stabilizing RanBP9 protein levels. Significance: Lowering COPS5 levels may be an effective therapeutic approach for AD.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Alzheimer's Disease (Ad)mentioning

confidence: 99%

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COPS5 (Jab1) Protein Increases β Site Processing of Amyloid Precursor Protein and Amyloid β Peptide Generation by Stabilizing RanBP9 Protein Levels

Wang

Dey

Carrera

et al. 2013

Journal of Biological Chemistry

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“…None of the original clones in the 2-hybrid screen encoded for RanBP9, although it is expressed in MKs and has been found in many screens using different baits. 34 The severe bleeding phenotype in RanBP10-null mice was originally attributed to impaired granule release in response to suboptimal concentrations of agonists 12 rather than to platelet spherocytosis, which has a weaker impact on platelet function. 18 Our data presented in this study rather suggest that lack of RanBP10 leads to a delayed contraction of the circumferential microtubule coil in response to threshold concentrations of platelet agonists that attenuates granule centralization and release ( Figure 5B-C).…”

Section: Impaired Thrombus Stability In Ranbp10-null Mice 3599mentioning

confidence: 99%

Altered microtubule equilibrium and impaired thrombus stability in mice lacking RanBP10

Meyer

Kunert

Schwiebert

et al. 2012

Blood

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The crucial function of blood platelets in hemostasis is to prevent blood loss by stable thrombus formation. This process is driven by orchestrated mechanisms including several signal transduction cascades and morphologic transformations. The cytoplasmic microtubule modulator RanBP10 is a Ran and ␤1-tubulin binding protein that is essential for platelet granule release and mice lacking RanBP10 harbor a severe bleeding phenotype. In this study, we demonstrate that RanBP10-nullizygous platelets show normal adhesion on collagen and von Willebrand factor under flow conditions. However, using a ferric chloride-induced arterial thrombosis model, the formation of stable thrombi was significantly impaired, preventing vessel occlusion or leading to recanalization and thromboembolization. Deltagranule secretion was normal in mutant mice, whereas platelet shape change in aggregometry was attenuated. Lack of RanBP10 leads to increased ␤1-tubulin protein, which drives ␣-monomers into polymerized microtubules. In mutant platelets agonists failed to contract the peripheral marginal band or centralize granules. Pretreatment of wild-type platelets with taxol caused microtubule stabilization and phenocopied the attenuated shape change in response to collagen, suggesting that RanBP10 inhibits premature microtubule polymerization of ␤1-tubulin and plays a pivotal role in thrombus stabilization. (Blood. 2012;120(17): 3594-3602) IntroductionMammals share a unique mechanism to ensure that injured blood vessels are sealed and loss of blood is minimized. Although specialized cells for this purpose are even found in invertebrates, the generation of anuclear cell fragments, designated platelets, are only present in mammals where they bud off cytoplasmic protrusions emanating from the megakaryocyte periphery. 1 These precursor cells form proplatelets and release nascent platelets across the endothelial barrier into the blood stream. 2 Endothelial cell lesions trigger platelets to make direct cellular contact with the subcellular matrix, which leads to platelet adhesion at the site of injury. Circulating platelets bind to an adhered layer of platelets, resulting in aggregation and thrombus formation, which is restricted to the site of injury and may ultimately occlude the vessel. 3 This process is tightly regulated as false activation leads to thrombosis and infarction, one of the major causes of death in the Western countries. Platelet activation is a multistep process. A hallmark of activation is the release of bioactive small molecules and proteins stored in 3 defined sets of granules present within the platelet cytoplasm: release of ␣-granules leads to surface expression of CD62P; CD63 is a marker for lysosomal granules; and dense granules harbor nucleotides such as ATP, ADP, amines, and bivalent cations. Although the granule markers are wellcharacterized, the molecular and cell biologic mechanisms underlying the process of granule release are less well understood. [4][5][6] Platelets harbor a cortical ring of bundled microtubules. In r...

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“…This is not surprising because most of the components contain LisH and CTLH protein domains that are known to mediate protein-protein interactions (Salemi et al, 2015). For example, to date, more than 50 protein interactions have been demonstrated for RanBPM (Francis et al, 2013;Suresh et al, 2012;Kobayashi et al, 2007). These proteins are involved in a variety of cellular processes, including cell adhesion and migration, microtubule dynamics, neuronal morphogenesis, male and female gametogenesis, gene transcription, regulation of protein stability, cell cycle regulation and other undefined cellular processes.…”

Section: Discussionmentioning

confidence: 99%

Integrative meta-analysis of protein interaction data identified multiple GID/MRCTLH protein complexes in plants

Miquel¹,

Vicient²

2017

Plant Omics

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GID/MRCTLH is a protein complex involved in the regulation of several cellular processes through the polyubiquitination and proteosome degradation. It has been described in yeast and mammals. Genes coding for homologous proteins are also present in plant genomes but have been little studied. BLAST analyses revealed that genes coding for members of the GID/MRCTLH complex are found in multiple copies in plants, compared to mammals and yeast. The potential structure of the Arabidopsis GID/MRCTLH complex was estimated based on the Arabidopsis protein interaction database Interactome 2.0. According to these data, Arabidopsis may contain two GID/MRCTLH complexes instead of the one described in yeast and mammals. The structure of the two Arabidopsis complexes seem to be similar to the yeast GID complex, and seem to interact with several other proteins out of the complex. These data suggest that, similarly to yeast and mammals, the plant GID/MRCTLH complexes are involved in the regulation of several cellular processes through proteosome protein degradation.

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Diverse roles of the scaffolding protein RanBPM

Cited by 38 publications

References 67 publications

COPS5 (Jab1) Protein Increases β Site Processing of Amyloid Precursor Protein and Amyloid β Peptide Generation by Stabilizing RanBP9 Protein Levels

COPS5 (Jab1) Protein Increases β Site Processing of Amyloid Precursor Protein and Amyloid β Peptide Generation by Stabilizing RanBP9 Protein Levels

Altered microtubule equilibrium and impaired thrombus stability in mice lacking RanBP10

Integrative meta-analysis of protein interaction data identified multiple GID/MRCTLH protein complexes in plants

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