Cofactors in and as posttranslational protein modifications.

FASEB J

Department of Nutrition, University of California, Davis 95616.

Published: April 1988

A symposium at the FASEB meeting in Las Vegas in May 1988 will be devoted to the role of cofactors (vitamins, coenzymes, prosthetic groups) in and as posttranslational protein modifications; the symposium is part of a thematic focus on metabolic regulation. In planning the symposium, we decided to consider metabolic regulation in its broadest context, which should include both the short-term activity modulations in the life of contemporary organisms and the adaptations of special molecular strategies over evolutionary time. We further decided to focus the symposium context on the involvement of cofactors both as catalytic participants in and as substrates or end products of posttranslational modifications. As a preview of the actual symposium, the present discussion is an attempt to enumerate cases of cofactor involvement in these different categories: 1) essential nutrients as participants in posttranslational modifications; 2) cofactors as donor substrates in reversible, regulatory modifications; and 3) cofactor incorporation or generation as covalent constituents of proteins. The actual symposium topics are taken from category 1: vitamin C and protein hydroxylation (K. I. Karivikkio) and vitamin K and protein carboxylation (J. W. Suttie) and category 3: biotinylation (H. G. Wood), phycobiliproteins (A. Glazer), and pyruvoyl enzymes (W. Dowhan).

Download full-text PDF

Source
http://dx.doi.org/10.1096/fasebj.2.7.3127264DOI Listing

Publication Analysis

Top Keywords

posttranslational protein
8
protein modifications
8
modifications symposium
8
metabolic regulation
8
posttranslational modifications
8
actual symposium
8
vitamin protein
8
symposium
6
modifications
5
cofactors
4

Similar Publications

The Shab family potassium channels are highly enriched at the presynaptic terminals of human neurons.

J Biol Chem

January 2025

Biochemistry & Molecular Biology, Colorado State University, Fort Collins, CO 80523, USA; Molecular, Cellular & Integrated Neurosciences, Colorado State University, Fort Collins, CO 80523, USA; Cell & Molecular Biology, Colorado State University, Fort Collins, CO 80523, USA. Electronic address:

The Shab family voltage-gated K channels (i.e., Kv2.

View Article and Find Full Text PDF

Protein mycoloylation is a newly characterized post-translational modification (PTM) specifically found in Corynebacteriales, an order of bacteria that includes numerous human pathogens. Their envelope is composed of a unique outer membrane, the so-called mycomembrane made of very-long chain fatty acids, named mycolic acids. Recently, some mycomembrane proteins including PorA have been unambiguously shown to be covalently modified with mycolic acids in the model organism Corynebacterium glutamicum by a mechanism that relies on the mycoloyltransferase MytC.

View Article and Find Full Text PDF

The γ-carboxylation of glutamate residues enables Ca-mediated membrane assembly of protein complexes that support broad physiological functions including hemostasis, calcium homeostasis, immune response, and endocrine regulation. Modulating γ-carboxylation level provides prevalent treatments for hemorrhagic and thromboembolic diseases. This unique posttranslational modification requires vitamin K hydroquinone (KH) to drive highly demanding reactions catalyzed by the membrane-integrated γ-carboxylase (VKGC).

View Article and Find Full Text PDF

Redox regulation of focal adhesions.

Redox Biol

January 2025

Redox Biology Group, Danish Cancer Institute, 2100, Copenhagen, Denmark. Electronic address:

Focal adhesions (FAs), multi-protein complexes that link the extracellular matrix to the intracellular cytoskeleton, are key mediators of cell adhesion, migration, and proliferation. These dynamic structures act as mechanical sensors, transmitting stimuli from the extracellular to intracellular environment activating in this way signaling pathways and enabling cells to adapt to environmental changes. As such, FAs are critical for tissue organization and serve as hubs governing cell spatial arrangement within the organism.

View Article and Find Full Text PDF

Regulation of pattern recognition receptor signaling by palmitoylation.

iScience

February 2025

Jiangsu Key Laboratory of Immunity and Metabolism, Department of Pathogenic Biology and Immunology, Xuzhou Medical University, Xuzhou, Jiangsu, China.

Pattern recognition receptors (PRRs), consisting of Toll-like receptors, RIG-I-like receptors, cytosolic DNA sensors, and NOD-like receptors, sense exogenous pathogenic molecules and endogenous damage signals to maintain physiological homeostasis. Upon activation, PRRs stimulate the sensitization of nuclear factor κB, mitogen-activated protein kinase, TANK-binding kinase 1-interferon (IFN) regulatory factor, and inflammasome signaling pathways to produce inflammatory factors and IFNs to activate Janus kinase/signal transducer and activator of transcription signaling pathways, resulting in anti-infection, antitumor, and other specific immune responses. Palmitoylation is a crucial type of post-translational modification that reversibly alters the localization, stability, and biological activity of target molecules.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!