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Related Concept Videos

Gap Junctions01:37

Gap Junctions

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Multicellular organisms employ a variety of ways for cells to communicate with each other. Gap junctions are specialized proteins that form pores between neighboring cells in animals, connecting the cytoplasm between the two, and allowing for the exchange of molecules and ions. They are found in a wide range of invertebrate and vertebrate species, mediate numerous functions including cell differentiation and development, and are associated with numerous human diseases, including cardiac and...
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Gap Junctions01:27

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The cytoplasm of adjacent animal cells can exchange small molecules, ions, and secondary messengers via the communication channels which form the gap junctions. These junctions comprise a few hundred to thousands of molecular channels, each made of two halves, called the connexon hemichannel. A connexon is a hexamer of six transmembrane connexin proteins, which assemble radially, thus forming a pore or channel in the center. One connexon hemichannel docks with a corresponding connexon on the...
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pH Regulation in Cells01:28

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pH plays a critical role in maintaining normal cellular activities. It helps maintain the structure and function of various proteins, dictates the charge on cellular membranes, and is crucial for metabolic reactions inside the cell. Moreover, cells use the energy from the proton motive force to generate ATP.
Cytosolic pH
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GTPases and their Regulation02:14

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Guanine nucleotide-binding proteins (G-proteins), also known as GTPases, are a superfamily of proteins that regulate many cellular processes, such as cell signaling, vesicular transport, and the regulation of cell shape and motility. Mutation or dysfunction of these proteins can lead to disease. There are around 40,000 known G-proteins that can broadly be classified into two groups ‒  small G-proteins consisting of a single domain and large multi-domain G-proteins.
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GTPases and their Regulation02:14

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Covalently Linked Protein Regulators02:04

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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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Cytosolic thiol switches regulating basic cellular functions: GAPDH as an information hub?

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    Cytosolic glyceraldehyde 3-phosphate dehydrogenase (GAPDH) acts as a redox sensor. Its oxidative modifications regulate metabolism, cellular functions, and cell fate decisions in response to cellular stress.

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    Area of Science:

    • Biochemistry
    • Cell Biology
    • Metabolic Regulation

    Background:

    • Cytosolic glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is a key glycolytic enzyme found in all organisms.
    • GAPDH is a primary target for oxidative modifications by reactive oxygen and nitrogen species.
    • Its catalytic cysteine residue is susceptible to various thiol modifications, including S-sulfenylation and S-glutathionylation.

    Purpose of the Study:

    • To review the mechanisms of GAPDH reactivity with hydrogen peroxide.
    • To explore the redox-dependent "moonlighting" functions of GAPDH.
    • To understand GAPDH's role in signaling adaptive responses, metabolic adjustment, or cell death.

    Main Methods:

    • Literature review focusing on recent discoveries.
    • Analysis of redox-dependent modifications of GAPDH.
    • Examination of GAPDH's diverse cellular roles beyond glycolysis.

    Main Results:

    • Oxidative modification of GAPDH reversibly inhibits glycolysis, diverting flux to the pentose-phosphate pathway for NADPH production.
    • Oxidized GAPDH exhibits novel functions in various cellular compartments, including the nucleus and cytoskeleton.
    • GAPDH's reactivity with H2O2 triggers distinct cellular outcomes, influencing metabolism and cell fate.

    Conclusions:

    • Cytosolic GAPDH functions as a critical sensor of cellular redox signals.
    • GAPDH acts as an information hub, transducing redox signals to orchestrate appropriate cellular responses.
    • These responses range from metabolic adaptation to programmed cell death, depending on the redox state.