Adenovirus core protein V interacts with p32--a protein which is associated with both the mitochondria and the nucleus.

Matthews, David A.; Russell, W. C.

doi:10.1099/0022-1317-79-7-1677

Cited by 178 publications

(186 citation statements)

References 32 publications

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“…As protein V had previously been shown to associate with the nucleolus and was excluded from the DBP-rich areas (Matthews & Russell, 1998a) we first assessed whether this also occurred with preMu-EGFP and Mu-EGFP protein ( Fig. 2A, B).…”

Section: Premu-egfp and Mu-egfp Were Excluded From The Dbp-rich Viralmentioning

confidence: 99%

Precursor of human adenovirus core polypeptide Mu targets the nucleolus and modulates the expression of E2 proteins

Lee

Lawrence

Dauksaite

et al. 2004

Journal of General Virology

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We have examined the subcellular localization properties of human adenovirus 2 (HAdV-2) preMu and mature Mu (pX) proteins as fusions with enhanced green fluorescence protein (EGFP). We determined that preMu is exclusively a nucleolar protein with a single nucleolar accumulation signal within the Mu sequence. In addition, we noted that both preMu-EGFP and Mu-EGFP are excluded from adenovirus DNA-binding protein (DBP)-rich replication centres in adenovirus-infected cells. Surprisingly, we observed that cells in which preMu-EGFP (but not Mu-EGFP) is transiently expressed prior to or shortly after infection with Ad2 did not express late adenovirus genes. Further investigation suggested this might be due to a failure to express pre-terminal protein (preTP) from the E2 region, despite expression of another E2 protein, DBP. Deletion mutagenesis identified a highly conserved region in the C terminus of preMu responsible for these observations. Thus our data suggest that preMu may play a role in modulating accumulation of proteins from the E2 region.

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Section: Premu-egfp and Mu-egfp Were Excluded From The Dbp-rich Viralmentioning

confidence: 99%

Precursor of human adenovirus core polypeptide Mu targets the nucleolus and modulates the expression of E2 proteins

Lee

Lawrence

Dauksaite

et al. 2004

Journal of General Virology

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“…It is found in the mitochondria (13)(14)(15), nucleus (14), cytoplasm (16,17) and at the cell surface (18)(19)(20). The N terminus of the immature gC1qR includes a mitochondrial targeting sequence.…”

mentioning

confidence: 99%

Inhibition of RIG-I and MDA5-dependent antiviral response by gC1qR at mitochondria

Xiao

Liu

et al. 2009

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

128

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“…1 It primarily localizes to the mitochondrial matrix, but has also been reported to be present in other subcellular locations. [2][3][4][5] Many human tumors exhibit higher p32 expression levels than their nonmalignant counterpart tissues. [6][7][8][9] Depleting p32 in human cancer cells strongly shifts their metabolism from oxidative phosphorylation to glycolysis.…”

mentioning

confidence: 99%

Chaperone-like protein p32 regulates ULK1 stability and autophagy

Jiao¹,

Gq²,

Dong³

et al. 2015

Cell Death Differ

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Mitophagy mediates clearance of dysfunctional mitochondria, and represents one type of mitochondrial quality control, which is essential for optimal mitochondrial bioenergetics. p32, a chaperone-like protein, is crucial for maintaining mitochondrial membrane potential and oxidative phosphorylation. However, the relationship between p32 and mitochondrial homeostasis has not been addressed. Here, we identified p32 as a key regulator of ULK1 stability by forming complex with ULK1. p32 depletion potentiated K48-linked but impaired K63-linked polyubiquitination of ULK1, leading to proteasome-mediated degradation of ULK1. As a result, silencing p32 profoundly impaired starvation-induced autophagic flux and the clearance of damaged mitochondria caused by mitochondrial uncoupler. Importantly, restoring ULK1 expression in p32-depleted cells rescued autophagy and mitophagy defects. Our findings highlight a cytoprotective role of p32 under starvation conditions by regulating ULK1 stability, and uncover a crucial role of the p32-ULK1-autophagy axis in coordinating stress response, cell survival and mitochondrial homeostasis. Mitophagy is a selective form of autophagy by which mitochondria are degraded in autolysosomes. p32 is a critical regulator of mitochondrial bioenergetics. 1 It primarily localizes to the mitochondrial matrix, but has also been reported to be present in other subcellular locations. 2-5 Many human tumors exhibit higher p32 expression levels than their nonmalignant counterpart tissues. 6-9 Depleting p32 in human cancer cells strongly shifts their metabolism from oxidative phosphorylation to glycolysis. 1 Consistently, p32 knockout causes mid-gestation lethality of knockout embryos and defects in oxidative phosphorylation. Mouse embryonic fibroblasts (MEFs) generated from p32 knockout embryos exhibited impaired ATP production and reduced mitochondrial membrane potential, which is in agreement with the observation that p32 silencing leads to increased mitochondrial fragmentation. 10,11 Notably, p32 was found to form protein complex with a variety of molecules 7,12,13 and has been suggested that it may act as a multifunctional chaperone protein. [12][13][14] ULK1 has a crucial role in mitophagy induction. 15 Despite the pivotal role of ULK1 in mitochondrial clearance, little is known as how ULK1 itself is regulated. ULK1 is a relatively stable protein and is subject to proteasome-mediated degradation. Post-translational modifications including K63-linked ubiquitylation 16,17 and phosphorylation [18][19][20] have been reported to modulate the rates of ULK1 turnover and kinase activity in different cellular contexts. Hsp90 and Cdc37 have been shown to regulate ULK1 stability and activity by forming complex with ULK1, which subsequently influences Atg13-mediated mitophagy. 21 Here, we found p32 regulates ULK1 stability by forming protein complex with ULK1. The interaction between ULK1 and p32 is crucial for maintaining the steady-state levels and activity of ULK1. We further show that p32 ablation results in a ...

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Adenovirus core protein V interacts with p32--a protein which is associated with both the mitochondria and the nucleus.

Cited by 178 publications

References 32 publications

Precursor of human adenovirus core polypeptide Mu targets the nucleolus and modulates the expression of E2 proteins

Precursor of human adenovirus core polypeptide Mu targets the nucleolus and modulates the expression of E2 proteins

Inhibition of RIG-I and MDA5-dependent antiviral response by gC1qR at mitochondria

Chaperone-like protein p32 regulates ULK1 stability and autophagy

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