Phosphatidylinositol 4,5-Diphosphate

myristoylated alanine rich protein kinase C substrate ; Homo sapiens







35 Article(s)
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1 33735912 MARCKS affects cell motility and response to BTK inhibitors in CLL. 2021 Aug 19 1
2 33958003 Pathophysiological roles of myristoylated alanine-rich C-kinase substrate (MARCKS) in hematological malignancies. 2021 May 6 1
3 34509657 The myristoylated alanine-rich C-kinase substrates (MARCKS): A membrane-anchored mediator of the cell function. 2021 Nov 2
4 32707323 MARCKS mediates vascular contractility through regulating interactions between voltage-gated Ca2+ channels and PIP2. 2020 Sep 4
5 30942445 Myristoylated alanine-rich C-kinase substrate effector domain phosphorylation regulates the growth and radiation sensitization of glioblastoma. 2019 Jun 2
6 29715315 A PKC-MARCKS-PI3K regulatory module links Ca2+ and PIP3 signals at the leading edge of polarized macrophages. 2018 2
7 27119641 Regulation of PI3K by PKC and MARCKS: Single-Molecule Analysis of a Reconstituted Signaling Pathway. 2016 Apr 26 2
8 27933776 Regulation of a Coupled MARCKS-PI3K Lipid Kinase Circuit by Calmodulin: Single-Molecule Analysis of a Membrane-Bound Signaling Module. 2016 Nov 22 5
9 25524703 Targeting the effector domain of the myristoylated alanine rich C-kinase substrate enhances lung cancer radiation sensitivity. 2015 Mar 4
10 26136560 Calmodulin and CaMKII modulate ENaC activity by regulating the association of MARCKS and the cytoskeleton with the apical membrane. 2015 Sep 1 2
11 26450120 Myristoylated Alanine-Rich Protein Kinase Substrate (MARCKS) Regulates Small GTPase Rac1 and Cdc42 Activity and Is a Critical Mediator of Vascular Smooth Muscle Cell Migration in Intimal Hyperplasia Formation. 2015 Oct 8 6
12 26470026 The Effector Domain of MARCKS Is a Nuclear Localization Signal that Regulates Cellular PIP2 Levels and Nuclear PIP2 Localization. 2015 7
13 24022404 Myristoylated alanine-rich C kinase substrate coordinates native TRPC1 channel activation by phosphatidylinositol 4,5-bisphosphate and protein kinase C in vascular smooth muscle. 2014 Jan 1
14 23704996 MARCKS protein is phosphorylated and regulates calcium mobilization during human acrosomal exocytosis. 2013 6
15 21097841 The MARCKS protein plays a critical role in phosphatidylinositol 4,5-bisphosphate metabolism and directed cell movement in vascular endothelial cells. 2011 Jan 21 1
16 21320438 Oscillations in the lateral pressure of lipid monolayers induced by nonlinear chemical dynamics of the second messengers MARCKS and protein kinase C. 2011 Feb 16 2
17 20651816 A possible role of myristoylated alanine-rich C kinase substrate in endocytic pathway of Alzheimer's disease. 2010 Aug 1
18 19362071 Interaction of the MARCKS peptide with PIP2 in phospholipid monolayers. 2009 Jul 3
19 19475567 MARCKS regulates lamellipodia formation induced by IGF-I via association with PIP2 and beta-actin at membrane microdomains. 2009 Sep 3
20 18186025 Matrix formalism for site-specific binding of unstructured proteins to multicomponent lipid membranes. 2008 Apr 1
21 18799624 Actin filament assembly by myristoylated alanine-rich C kinase substrate-phosphatidylinositol-4,5-diphosphate signaling is critical for dendrite branching. 2008 Nov 3
22 15649142 Reversible - through calmodulin - electrostatic interactions between basic residues on proteins and acidic lipids in the plasma membrane. 2005 2
23 15041659 Electrostatic sequestration of PIP2 on phospholipid membranes by basic/aromatic regions of proteins. 2004 Apr 3
24 15052337 The MARCKS family of phospholipid binding proteins: regulation of phospholipase D and other cellular components. 2004 Feb 4
25 15298909 Fluorescence correlation spectroscopy studies of Peptide and protein binding to phospholipid vesicles. 2004 Aug 1
26 12670959 Binding of peptides with basic and aromatic residues to bilayer membranes: phenylalanine in the myristoylated alanine-rich C kinase substrate effector domain penetrates into the hydrophobic core of the bilayer. 2003 Jun 13 2
27 11825894 Myristoylated alanine-rich C kinase substrate (MARCKS) sequesters spin-labeled phosphatidylinositol 4,5-bisphosphate in lipid bilayers. 2002 Apr 19 2
28 11988466 PIP(2) and proteins: interactions, organization, and information flow. 2002 1
29 11053422 The effector domain of myristoylated alanine-rich C kinase substrate binds strongly to phosphatidylinositol 4,5-bisphosphate. 2001 Feb 16 1
30 10956022 Membrane binding of peptides containing both basic and aromatic residues. Experimental studies with peptides corresponding to the scaffolding region of caveolin and the effector region of MARCKS. 2000 Aug 22 2
31 9533686 Binding of basic peptides to membranes produces lateral domains enriched in the acidic lipids phosphatidylserine and phosphatidylinositol 4,5-bisphosphate: an electrostatic model and experimental results. 1998 Feb 4
32 9259558 MARCKS regulates membrane ruffling and cell spreading. 1997 Aug 1 3
33 9341159 Kinetics of interaction of the myristoylated alanine-rich C kinase substrate, membranes, and calmodulin. 1997 Oct 24 2
34 8611023 Binding of myristoylated alanine-rich protein kinase C substrate to phosphoinositides attenuates the phosphorylation by protein kinase C. 1996 Feb 15 1
35 8824266 Myristoylated alanine-rich C kinase substrate (MARCKS) produces reversible inhibition of phospholipase C by sequestering phosphatidylinositol 4,5-bisphosphate in lateral domains. 1996 Oct 18 5