Succinylation of Pepsinogen

Gounaris, Anne D.; Perlmann, Gertrude E.

doi:10.1016/s0021-9258(18)99630-4

Cited by 159 publications

(41 citation statements)

References 19 publications

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“…Research on succinylation stemmed from its role in inhibiting antibody formation and testing allergic skin responses in animals that were sensitive to dinitrophenyl-polyline in 1962 (Parker et al, 1962 ). In the following years, the succinylation of pepsinogen (Gounaris and Perlmann, 1967 ), ovalbumin (Kidwai et al, 1976 ), and histone amino groups (Pineiro et al, 1992 ) was studied in succession. However, it was not until 2011 that succinylation was identified as a natural PTM of lysine residues in bacteria by affinity purification with anti-succinyl lysine antibody (Zhang et al, 2011 ; Alleyn et al, 2018 ; Sreedhar et al, 2020 ).…”

Section: Metabolites Play Key Roles In Epigenetic Remodeling On the P...mentioning

confidence: 99%

Metabolic reprogramming and epigenetic modifications on the path to cancer

2021

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Metabolic rewiring and epigenetic remodeling, which are closely linked and reciprocally regulate each other, are among the well-known cancer hallmarks. Recent evidence suggests that many metabolites serve as substrates or cofactors of chromatin-modifying enzymes as a consequence of the translocation or spatial regionalization of enzymes or metabolites. Various metabolic alterations and epigenetic modifications also reportedly drive immune escape or impede immunosurveillance within certain contexts, playing important roles in tumor progression. In this review, we focus on how metabolic reprogramming of tumor cells and immune cells reshapes epigenetic alterations, in particular the acetylation and methylation of histone proteins and DNA. We also discuss other eminent metabolic modifications such as, succinylation, hydroxybutyrylation, and lactylation, and update the current advances in metabolism- and epigenetic modification-based therapeutic prospects in cancer.

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Section: Metabolites Play Key Roles In Epigenetic Remodeling On the P...mentioning

confidence: 99%

Metabolic reprogramming and epigenetic modifications on the path to cancer

2021

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“…Carboxylate modified latex microbeads (Invitrogen, Waltham, MA, USA) were coated with reOmpB using published protocols [63,64]. Briefly, microbeads were suspended in 2-(N-morpholino) ethanesulfonic acid (MES) buffer.…”

Section: Fluidfm Adhesion Assaymentioning

confidence: 99%

Host EPAC1 Modulates Rickettsial Adhesion to Vascular Endothelial Cells via Regulation of ANXA2 Y23 Phosphorylation

Shelite

Qiu

et al. 2021

Pathogens

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Introduction: Intracellular cAMP receptor exchange proteins directly activated by cAMP 1 (EPAC1) regulate obligate intracellular parasitic bacterium rickettsial adherence to and invasion into vascular endothelial cells (ECs). However, underlying precise mechanism(s) remain unclear. The aim of the study is to dissect the functional role of the EPAC1-ANXA2 signaling pathway during initial adhesion of rickettsiae to EC surfaces. Methods: In the present study, an established system that is anatomically based and quantifies bacterial adhesion to ECs in vivo was combined with novel fluidic force microscopy (FluidFM) to dissect the functional role of the EPAC1-ANXA2 signaling pathway in rickettsiae–EC adhesion. Results: The deletion of the EPAC1 gene impedes rickettsial binding to endothelium in vivo. Rickettsial OmpB shows a host EPAC1-dependent binding strength on the surface of a living brain microvascular EC (BMEC). Furthermore, ectopic expression of phosphodefective and phosphomimic mutants replacing tyrosine (Y) 23 of ANXA2 in ANXA2-knock out BMECs results in different binding force to reOmpB in response to the activation of EPAC1. Conclusions: EPAC1 modulates rickettsial adhesion, in association with Y23 phosphorylation of the binding receptor ANXA2. Underlying mechanism(s) should be further explored to delineate the accurate role of cAMP-EPAC system during rickettsial infection.

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“…Carboxylate modified latex microbeads (5 µm CML Latex Beads, Invitrogen) were coated with reOmpB using published protocols (20,21). Briefly, microbeads were suspended in 2-(Nmorpholino) ethanesulfonic acid (MES) buffer.…”

Section: Fluidfm Adhesion Assaymentioning

confidence: 99%

Host EPAC1 modulates rickettsial adhesion to vascular endothelial cells via regulation of ANXA2 Y23 phosphorylation

Shelite

Qiu

et al. 2021

Preprint

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Recently we have identified that endothelial surface annexin A2 (ANAX2) functions as a receptor for spotted fever group rickettsial adhesin outer membrane protein B (OmpB), which binds to the endothelial cell (EC) surface. Moreover, we reported that intracellular cAMP receptor EPAC1 modulates ANXA2 tyrosine (Y) 23 phosphorylation, and inactivation of EPAC1 suppresses ANXA2 expression on the EC luminal surface by downregulating Y23 phosphorylation. Since we reported that EPAC1 plays a critical role in the initial step to successfully establish rickettsial infection of ECs, this work aims to answer the following: (a) What is the mechanism underlying the regulatory role of EPAC1 in ECs during the initial step of bacterial infection? (b) Is the EPAC1-ANXA2 signaling pathway involved in the regulation of rickettsial adhesion to ECs?In the present study, an established system that is anatomically-based and quantifies bacterial adhesion to ECs in vivo was combined with novel fluidic force microscopy (FluidFM) to dissect the functional role of the EPAC1-ANXA2 signaling pathway in rickettsiae–EC adhesion. We reveal that the deletion of the EPAC1 gene impedes rickettsial binding to endothelium in vivo. In addition, single living brain microvascular EC study that employs FluidFM and site-directed mutagenesis provides evidence that supports our finding that EPAC1 governs rickettsial adhesion to EC surfaces via regulation of ANXA2 Y23 phosphorylation.

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Succinylation of Pepsinogen

Cited by 159 publications

References 19 publications

Metabolic reprogramming and epigenetic modifications on the path to cancer

Metabolic reprogramming and epigenetic modifications on the path to cancer

Host EPAC1 Modulates Rickettsial Adhesion to Vascular Endothelial Cells via Regulation of ANXA2 Y23 Phosphorylation

Host EPAC1 modulates rickettsial adhesion to vascular endothelial cells via regulation of ANXA2 Y23 phosphorylation

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