23 Replies to “Susan Taylor (UCSD) Part 1: Protein Phosphorylation in Biology”

  1. IκBs are a family of related proteins that have an N-terminal regulatory domain, followed by six or more ankyrin repeats and a PEST domain near their C terminus. IκBα is the best-studied and major IκB protein.

  2. Great video lecture!!. Performing phosphoproteomics research on biopsy material from cancer patients. Its good to back to the basics for a good understanding.
    Especially the historic context is very interesting.
    Has someone ever written a book about the history of molecular biology ??

  3. #Kinases transfer the γ-phosphate of ATP to other biological molecules, serving as chemical messengers that make the tight regulation of cell-signaling pathways possible. For example, non-receptor tyrosine kinases are found in the cytoplasm (not membrane-bound) and transfer the γ-phosphate of ATP to tyrosine residues of other proteins, often turning these proteins “on” or “off” in the context of their respective signaling pathway. This notion of “on” or “off” can be useful to holistically conceptualize these pathways but is a gross oversimplification; in reality, many of these enzymes are multi-domain proteins that can exist in multiple conformational states, participate in multiple protein-protein interactions, and experience a gradient of variable activity levels depending on these states. The molecular mechanisms that govern the activity of these kinases is extraordinarily complex, and though much has been discovered in recent years, much remains to be understood, especially for the Tec family of non-receptor tyrosine kinases.

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