Convergent signaling pathways—interaction between methionine oxidation and serine/threonine/tyrosine O-phosphorylation

Rao, R. Shyama Prasad; Thelen, Jay J.; Miernyk, Ján A.

doi:10.1007/s12192-014-0544-1

Cited by 16 publications

(12 citation statements)

References 67 publications

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“…Methionine residues are reported to interact with tyrosine residues (39). The phenolic group of tyrosine is also capable of attacking the sulfhydryl position of methionine during acid catalysis (40,41). Additionally, oxidized methionine residues have been shown to alter O-linked phosphorylations as well as affect HIV-2 protease activity (41,42).…”

Section: Discussionmentioning

confidence: 99%

“…The phenolic group of tyrosine is also capable of attacking the sulfhydryl position of methionine during acid catalysis (40,41). Additionally, oxidized methionine residues have been shown to alter O-linked phosphorylations as well as affect HIV-2 protease activity (41,42). Thus, the presence of M63 provides a large potential of putative p12 N-to C-terminal interactions, which would be absent in the p12-I63 constructs.…”

Section: Discussionmentioning

confidence: 99%

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Repression of the Chromatin-Tethering Domain of Murine Leukemia Virus p12

Brzezinski

Modi

Liu

et al. 2016

J Virol

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Murine leukemia virus (MLV) p12, encoded within Gag, binds the viral preintegration complex (PIC) to the mitotic chromatin. This acts to anchor the viral PIC in the nucleus as the nuclear envelope re-forms postmitosis. Mutations within the p12 C terminus (p12 PM13 to PM15) block early stages in viral replication. Within the p12 PM13 region (p12 60 PSPMA 65 ), our studies indicated that chromatin tethering was not detected when the wild-type (WT) p12 protein (M63) was expressed as a green fluorescent protein (GFP) fusion; however, constructs bearing p12-I63 were tethered. N-terminal truncations of the activated p12-I63-GFP indicated that tethering increased further upon deletion of p12 25 DLLTEDPPPY 34 , which includes the late domain required for viral assembly. The p12 PM15 sequence (p12 70 RREPP 74 ) is critical for wild-type viral viability; however, virions bearing the PM15 mutation (p12 70 AAAAA 74 ) with a second M63I mutant were viable, with a titer 18-fold lower than that of the WT. The p12 M63I mutation amplified chromatin tethering and compensated for the loss of chromatin binding of p12 PM15. Rescue of the p12-M63-PM15 nonviable mutant with prototype foamy virus (PFV) and Kaposi's sarcoma herpesvirus (KSHV) tethering sequences confirmed the function of p12 70 -74 in chromatin binding. Minimally, full-strength tethering was seen with only p12 61 SPIASRLRGRR 71 fused to GFP. These results indicate that the p12 C terminus alone is sufficient for chromatin binding and that the presence of the p12 25 DLLTEDPPPY 34 motif in the N terminus suppresses the ability to tether. IMPORTANCEThis study defines a regulatory mechanism controlling the differential roles of the MLV p12 protein in early and late replication. During viral assembly and egress, the late domain within the p12 N terminus functions to bind host vesicle release factors. During viral entry, the C terminus of p12 is required for tethering to host mitotic chromosomes. Our studies indicate that the p12 domain including the PPPY late sequence temporally represses the p12 chromatin tethering motif. Maximal p12 tethering was identified with only an 11-amino-acid minimal chromatin tethering motif encoded at p12 61-71 . Within this region, the p12-M63I substitution switches p12 into a tethering-competent state, partially rescuing the p12-PM15 tethering mutant. A model for how this conformational change regulates early versus late functions is presented.T he p12 structural protein of murine leukemia virus (MLV) was recently identified as a critical chromatin tether for the early viral life cycle. MLV requires cells to undergo mitosis to gain nuclear entry and requires a mechanism to remain nuclear after mitosis is complete, since integration occurs after exit from mitosis (1, 2). p12 accomplishes this by binding the viral preintegration complex (PIC) with its N terminus (3) and nuclear chromatin with its C terminus (2-4). This p12 chromatin binding motif was shown to not affect MLV integration targeting to transcriptional start sites (4), and inte...

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Repression of the Chromatin-Tethering Domain of Murine Leukemia Virus p12

Brzezinski

Modi

Liu

et al. 2016

J Virol

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“…These changes were accompanied by alterations in hepatic mRNA and protein levels of apoAI, SR-BI, ABCA1, ABCG8, and LXRα, as well as key enzymes such as CYP7A1, CYP27A1, CEH, and ACAT. These effects of hepatic MsrA may involve the modulation of the interaction between Met oxidation and cellular signaling, such as protein kinase/phosphatase-based signaling ( 23 ).…”

Section: Discussionmentioning

confidence: 99%

Hepatic overexpression of methionine sulfoxide reductase A reduces atherosclerosis in apolipoprotein E-deficient mice

Meng

et al. 2015

Journal of Lipid Research

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Methionine sulfoxide reductase A (MsrA), a specific enzyme that converts methionine-S-sulfoxide to methionine, plays an important role in the regulation of protein function and the maintenance of redox homeostasis. In this study, we examined the impact of hepatic MsrA overexpression on lipid metabolism and atherosclerosis in apoE-deficient (apoE−/−) mice. In vitro study showed that in HepG2 cells, lentivirus-mediated human MsrA (hMsrA) overexpression upregulated the expression levels of several key lipoprotein-metabolism-related genes such as liver X receptor α, scavenger receptor class B type I, and ABCA1. ApoE−/− mice were intravenously injected with lentivirus to achieve high-level hMsrA expression predominantly in the liver. We found that hepatic hMsrA expression significantly reduced plasma VLDL/LDL levels, improved plasma superoxide dismutase, and paraoxonase-1 activities, and decreased plasma serum amyloid A level in apoE−/− mice fed a Western diet, by significantly altering the expression of several genes in the liver involving cholesterol selective uptake, conversion and excretion into bile, TG biosynthesis, and inflammation. Moreover, overexpression of hMsrA resulted in reduced hepatic steatosis and aortic atherosclerosis. These results suggest that hepatic MsrA may be an effective therapeutic target for ameliorating dyslipidemia and reducing atherosclerosis-related cardiovascular diseases.

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“…Not only are there many different PTMs, each of which can affect the structure and function of the same protein, but also these regulatory PTMs can also interact. A case in point is protein phosphorylation, which we now know can be modulated by oxidation of adjacent methionine residues (Rao et al ). An interesting point is that the two ICDHs mentioned earlier are both phosphorylated and acetylated indicating that these two PTMs interact with thioredoxin regulation in the control of mitochondrial metabolism (Bykova et al , Balmer et al , Møller ).…”

Section: The Study Of Posttranslational Modification Of Proteins Is Tmentioning

confidence: 99%

What is hot in plant mitochondria?

Møller

2016

Physiologia Plantarum

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In this overview of recent trends in plant mitochondrial research, four questions are considered: (1) How large is the mitochondrial proteome? It appears to be in excess of 1500 proteins in a tissue at any given time. It is proposed that the fusion-fission frequently observed for plant mitochondria provides a vital mixing function ensuring that all low-abundance proteins are present in each mitochondrion at least some of the time. (2) What is the significance of posttranslational modifications (PTM) of proteins? As a result of PTM, many proteins are present in a very large number of slightly different forms. The most well-studied PTMs, such as protein phosphorylation, acetylation and reversible cysteine oxidation, are known to regulate mitochondrial function. Recent studies have provided examples of the importance of this regulation, but it remains a research area with a massive growth potential. (3) What is the role(s) of pentatricopeptide repeat (PPR) proteins in plant mitochondria? There is general agreement that PPR proteins are involved in RNA metabolism such as RNA editing. Recent comprehensive proteomic studies raise the question of how many of the potential 250-300 mitochondrial PPR proteins encoded in the nuclear DNA are required to be present for a mitochondrion to be able to grow and divide. (4) What is the mechanism(s) of retrograde signal transduction from the mitochondria to the nucleus? The nature of the signal transduction molecule is still unknown, but calcium ions, hydrogen peroxide and/or oxidized peptides are potential candidates. Recent results place a receptor for the activation of a group of nuclear genes on the endoplasmic reticulum, possibly close to ER-mitochondrial contact points.

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Convergent signaling pathways—interaction between methionine oxidation and serine/threonine/tyrosine O-phosphorylation

Cited by 16 publications

References 67 publications

Repression of the Chromatin-Tethering Domain of Murine Leukemia Virus p12

Repression of the Chromatin-Tethering Domain of Murine Leukemia Virus p12

Hepatic overexpression of methionine sulfoxide reductase A reduces atherosclerosis in apolipoprotein E-deficient mice

What is hot in plant mitochondria?

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