Purification of a Phosphatidylinositol 4-Phosphate Kinase from Bovine Brain Membranes

Author:

Moritz Albrecht,Graan Pierre N. E.,Ekhart Peter F.,Gispen Willem H.,Wirtz Karel W. A.

Publisher

Wiley

Subject

Cellular and Molecular Neuroscience,Biochemistry

Cited by 33 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

1. Signaling roles of phosphoinositides in the retina;Journal of Lipid Research;2021

2. PIP4K and the role of nuclear phosphoinositides in tumour suppression;Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids;2015-06

3. Regulation of Phosphatidylinositol 4-Phosphate 5-Kinase Activity by Partner Proteins;Methods in Enzymology;2007

4. Regulation of Type II Phosphatidylinositol Phosphate Kinase by Tyrosine Phosphorylation in Bovine Rod Outer Segments;Biochemistry;2001-03-22

5. PIPkins1We introduce here the abbreviation PIPkin (an abbreviation we have used in our lab for years) for cogent reasons. Previously, PtdIns4P 5-kinase was the favoured abbreviation, but in view of the extensive revision and uncertainty as to substrates and products that we discuss in this review, only PtdInsP kinase would now suffice. Moreover, we have recently recorded evidence that type II PIPkin is subject to multiple phosphorylations by protein kinases [1]. As we progress in our characterisation of these kinases, we feel that ‘PtdInsP kinase kinases’ is a very confusing term for them, and using PIPkins for PtdInsP kinases (and thus PIPkin kinases for the protein kinases that phosphorylate them) is much to be preferred for general use. A fuller abbreviation, where the reaction catalysed is known, e.g. type I PtdIns4P 5-kinase, is of course a suitable alternative in many instances.1, their substrates and their products: new functions for old enzymes;Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids;1998-12

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