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Polypyrimidine tract-binding protein, also known as PTB or hnRNP I, is an RNA-binding protein. PTB functions mainly as a splicing regulator, although it is also involved in alternative 3' end processing, mRNA stability and RNA localization. [ 1 ]
PTBP1 has been shown to interact with HNRPK, [9] PCBP2, [9] SFPQ [10] [11] and HNRNPL. [9] [12]This gene is targeted by the microRNA miR-124.During neuronal differentiation, miR-124 reduces PTBP1 levels, leading to the accumulation of correctly spliced PTBP2 mRNA and a dramatic increase in PTBP2 protein.
The PTB domains facilitate interaction with the activated tyrosine-phosphorylated insulin receptor. The PTB domain is situated towards the N terminus . Two arginines in this domain are responsible for hydrogen bonding phosphotyrosine residues on an Ac -LYASSNPApY- NH2 peptide in the juxtamembrane region of the insulin receptor.
Molecular Biology of the Cell has been described as "the most influential cell biology textbook of its time". [2] The sixth edition is dedicated to the memory of co-author Julian Lewis, who died in early 2014. The book was the first to position cell biology as a central discipline for biology and medicine, and immediately became a landmark ...
This page was last edited on 24 February 2022, at 23:06 (UTC).; Text is available under the Creative Commons Attribution-ShareAlike 4.0 License; additional terms may apply.
In 1988, Lewis C. Cantley published a paper describing the discovery of a novel type of phosphoinositide kinase with the unprecedented ability to phosphorylate the 3' position of the inositol ring resulting in the formation of phosphatidylinositol-3-phosphate (PI3P). [1]
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Biology I from cells to organisms Institution First Nations University Instructor Jeff Racette Wikipedia Expert Ian (Wiki Ed) Subject Genes and Proteins Course dates 2024-09-05 00:00:00 UTC – 2024-12-05 23:59:59 UTC Approximate number of student editors 36