Vaults and the major vault protein: Novel roles in signal pathway regulation and immunity

Berger, Walter; Steiner, Elisabeth; Grusch, Michael; Elbling, Leonilla; Micksche, M.

doi:10.1007/s00018-008-8364-z

Cited by 212 publications

(231 citation statements)

References 149 publications

(322 reference statements)

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“…1C). Although the functions of TbArmtor and MVP proteins in trypanosomes are unknown, it has been shown previously that an MVP complex serves as a kinase scaffold (14,15). These results suggest that TbTOR4 forms a structurally unique complex that we named "TbTORC4."…”

mentioning

confidence: 77%

Third target of rapamycin complex negatively regulates development of quiescence in Trypanosoma brucei

Barquilla

Saldivia

Díaz

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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African trypanosomes are protozoan parasites transmitted by a tsetse fly vector to a mammalian host. The life cycle includes highly proliferative forms and quiescent forms, the latter being adapted to host transmission. The signaling pathways controlling the developmental switch between the two forms remain unknown. Trypanosoma brucei contains two target of rapamycin (TOR) kinases, TbTOR1 and TbTOR2, and two TOR complexes, TbTORC1 and TbTORC2. Surprisingly, two additional TOR kinases are encoded in the T. brucei genome. We report that TbTOR4 associates with an Armadillo domain-containing protein (TbArmtor), a major vault protein, and LST8 to form a unique TOR complex, TbTORC4. Depletion of TbTOR4 caused irreversible differentiation of the parasite into the quiescent form. AMP and hydrolysable analogs of cAMP inhibited TbTOR4 expression and induced the stumpy quiescent form. Our results reveal unexpected complexity in TOR signaling and show that TbTORC4 negatively regulates differentiation of the proliferative form into the quiescent form.parasitology | cell biology | kinetoplastida

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mentioning

confidence: 77%

Third target of rapamycin complex negatively regulates development of quiescence in Trypanosoma brucei

Barquilla

Saldivia

Díaz

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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“…40,41 VtRNAs are components of the vault complex, a hollow, barrel-shaped ribonucleoprotein complex that is thought to play a role in cellular resistance to cancer therapeutic (for a review see ref. 42). However, the exact role of vtRNAs, as well as the vault complex, is not yet clear.…”

Section: Discussionmentioning

confidence: 99%

Upregulation of a small vault RNA (svtRNA2-1a) is an early event in Parkinson disease and induces neuronal dysfunction

et al. 2013

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“…Despite 20 years of research, the exact function of MVP is still unclear. Vault complexes are implicated in the cellular response to environmental toxins (Berger et al, 2009). They also bind to several effectors of signaling cascades that are stress induced, such as the pro-apoptotic phospholipid phosphatase PTEN (phosphatase and tensin homolog) pathway, an antagonist of the phosphatidylinositol 3-kinase, and the epidermal growth factor (EGFR)-induced MAPK pathway (Berger et al, 2009).…”

Section: Signaling Proteinsmentioning

confidence: 99%

The proteomic response of the mussel congenersMytilus galloprovincialisandM. trossulusto acute heat stress: implications for thermal tolerance limits and metabolic costs of thermal stress

Tomanek

Zuzow

2010

Journal of Experimental Biology

265

273

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SUMMARYThe Mediterranean blue mussel, Mytilus galloprovincialis, an invasive species in California, has displaced the more heat-sensitive native congener, Mytilus trossulus, from its former southern range, possibly due to climate change. By comparing the response of their proteomes to acute heat stress we sought to identify responses common to both species as well as differences that account for greater heat tolerance in the invasive. Mussels were acclimated to 13°C for four weeks and exposed to acute heat stress (24°C, 28°C and 32°C) for 1h and returned to 13°C to recover for 24h. Using two-dimensional gel electrophoresis and tandem mass spectrometry we identified 47 and 61 distinct proteins that changed abundance in M. galloprovincialis and M. trossulus, respectively. The onset temperatures of greater abundance of some members of the heat shock protein (Hsp) 70 and small Hsp families were lower in M. trossulus. The abundance of proteasome subunits was lower in M. galloprovincialis but greater in M. trossulus in response to heat. Levels of several NADH-metabolizing proteins, possibly linked to the generation of reactive oxygen species (ROS), were lower at 32°C in the cold-adapted M. trossulus whereas proteins generating NADPH, important in ROS defense, were higher in both species. The abundance of oxidative stress proteins was lower at 32°C in M. trossulus only, indicating that its ability to combat heat-induced oxidative stress is limited to lower temperatures. Levels of NADdependent deacetylase (sirtuin 5), which are correlated with lifespan, were lower in M. trossulus in response to heat stress. In summary, the expression patterns of proteins involved in molecular chaperoning, proteolysis, energy metabolism, oxidative damage, cytoskeleton and deacetylation revealed a common loci of heat stress in both mussels but also showed a lower sensitivity to high-temperature damage in the warm-adapted M. galloprovincialis, which is consistent with its expanding range in warmer waters. Supplementary material available online at

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Vaults and the major vault protein: Novel roles in signal pathway regulation and immunity

Cited by 212 publications

References 149 publications

Third target of rapamycin complex negatively regulates development of quiescence in Trypanosoma brucei

Third target of rapamycin complex negatively regulates development of quiescence in Trypanosoma brucei

Upregulation of a small vault RNA (svtRNA2-1a) is an early event in Parkinson disease and induces neuronal dysfunction

The proteomic response of the mussel congenersMytilus galloprovincialisandM. trossulusto acute heat stress: implications for thermal tolerance limits and metabolic costs of thermal stress

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