Type IIα phosphatidylinositol phosphate kinase associates with the plasma membrane via interaction with type I isoforms

2002 ◽  
Vol 363 (3) ◽  
pp. 563-570 ◽  
Author(s):  
Katherine A. HINCHLIFFE ◽  
Maria Luisa GIUDICI ◽  
Andrew J. LETCHER ◽  
Robin F. IRVINE
Keyword(s):  
Plasma Membrane ◽  
Substrate Specificity ◽  
Subcellular Localization ◽  
Physiological Function ◽  
Distinct Type ◽  
Type I ◽  
Type Ii ◽  
Phosphatidylinositol Phosphate ◽  
Inositol Phospholipids ◽  
Inositol Lipids

The phosphatidylinositol phosphate kinases (PIPkins) are a family of enzymes involved in regulating levels of several functionally important inositol phospholipids within cells. The PIPkin family is subdivided into three on the basis of substrate specificity, each subtype presumably regulating levels of different subsets of the inositol lipids. The physiological function of the type II isoforms, which exhibit a preference for phosphatidylinositol 5-phosphate, a lipid about which very little is known, is particularly poorly understood. In the present study, we demonstrate interaction between, and co-immunoprecipitation of, type IIα PIPkin with the related, but biochemically and immunologically distinct, type I PIPkin isoforms. Type IIα PIPkin interacts with all three known type I PIPkins (α, β and γ), and in each case co-expression of the type I isoform with type IIα results in recruitment of the latter from the cytosol to the plasma membrane of the cell. This change in subcellular localization could result in improved access of the type IIα PIPkin to its lipid substrates.

scholarly journals Plasma membrane processes are differentially regulated by type I phosphatidylinositol phosphate 5-kinases and RASSF4

2019 ◽  
Vol 133 (2) ◽  
pp. jcs233254 ◽  
Author(s):  
Lizbeth de la Cruz ◽  
Alexis Traynor-Kaplan ◽  
Oscar Vivas ◽  
Bertil Hille ◽  
Jill B. Jensen
Keyword(s):  
Plasma Membrane ◽  
Type I ◽  
Membrane Processes ◽  
Phosphatidylinositol Phosphate

scholarly journals Stat-mediated Signaling Induced by Type I and Type II Interferons (IFNs) Is Differentially Controlled through Lipid Microdomain Association and Clathrin-dependent Endocytosis of IFN Receptors

2006 ◽  
Vol 17 (7) ◽  
pp. 2896-2909 ◽  
Author(s):  
Marta Marchetti ◽  
Marie-Noelle Monier ◽  
Alexandre Fradagrada ◽  
Keith Mitchell ◽  
Florence Baychelier ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Biological Activities ◽  
Critical Role ◽  
Membrane Lipid ◽  
Endocytic Pathway ◽  
Type I ◽  
Type Ii ◽  
Biological Responses ◽  
Signal Specificity ◽  
Ifn Γ

Type I (α/β) and type II (γ) interferons (IFNs) bind to distinct receptors, although they activate the same signal transducer and activator of transcription, Stat1, raising the question of how signal specificity is maintained. Here, we have characterized the sorting of IFN receptors (IFN-Rs) at the plasma membrane and the role it plays in IFN-dependent signaling and biological activities. We show that both IFN-α and IFN-γ receptors are internalized by a classical clathrin- and dynamin-dependent endocytic pathway. Although inhibition of clathrin-dependent endocytosis blocked the uptake of IFN-α and IFN-γ receptors, this inhibition only affected IFN-α–induced Stat1 and Stat2 signaling. Furthermore, the antiviral and antiproliferative activities induced by IFN-α but not IFN-γ were also affected. Finally, we show that, unlike IFN-α receptors, activated IFN-γ receptors rapidly become enriched in plasma membrane lipid microdomains. We conclude that IFN-R compartmentalization at the plasma membrane, through clathrin-dependent endocytosis and lipid-based microdomains, plays a critical role in the signaling and biological responses induced by IFNs and contributes to establishing specificity within the Jak/Stat signaling pathway.

scholarly journals Identification of actin-, alpha-actinin-, and vinculin-containing plaques at the lateral membrane of epithelial cells.

1986 ◽  
Vol 102 (5) ◽  
pp. 1843-1852 ◽  
Author(s):  
D Drenckhahn ◽  
H Franz
Keyword(s):  
Plasma Membrane ◽  
Cross Sections ◽  
Three Dimensional ◽  
Intercellular Junctions ◽  
Classical Type ◽  
Type I ◽  
Type Ii ◽  
Microscopic Studies ◽  
Prostatic Epithelium ◽  
Human Intestinal Epithelium

In this paper, a new type of spot desmosome-like junction (type II plaque) is described that is scattered along the entire lateral plasma membrane of rat and human intestinal epithelium. Ultrastructurally type II plaques differed from the classical type of epithelial spot desmosome ("macula adherens", further denoted as type I desmosome) by weak electron density of the membrane-associated plaque material, association of the plaques with microfilaments rather than intermediate filaments, and poorly visible material across the intercellular space. Thus, type II plaques resemble cross-sections of the zonula adherens. Immunofluorescence-microscopic studies were done using antibodies to a main protein associated with the plaques of type I desmosomes (desmoplakin I) and to the three major proteins located at the plaques of the zonula adherens (actin, alpha-actinin, and vinculin). Two types of plaques were visualized along the lateral surface of intestinal and prostatic epithelium: (a) the type I desmosomes, which were labeled with anti-desmoplakin but did not bind antibodies to actin, alpha-actinin, and vinculin, and (b) a further set of similarly sized plaques, which bound antibodies to actin, alpha-actinin, and vinculin but were not stained with anti-desmoplakin. Three-dimensional computer reconstruction of serial sections double-labeled with anti-desmoplakin and anti-alpha-actinin further confirmed that both types of plaques are spatially completely separated from each other along the lateral plasma membrane. The computer graphs further revealed that the actin-, alpha-actinin-, and vinculin-containing plaques have the tendency to form clusters, a feature also typical of type II plaques. It is suggested that the type II plaques represent spot desmosome-like intercellular junctions, which, like the zonula adherens, appear to be linked to the actin filament system. As the type II plaques cover a considerable part of the lateral cell surface, they might play a particular role in controlling cellular shape and intercellular adhesion.

Comparison of the substrate specificity of type I and type II dehydroquinases with 5-deoxy- and 4,5-dideoxy-dehydroquinic acid

1996 ◽  
pp. 2371 ◽  
Author(s):  
Joanna M. Harris ◽  
William J. Watkins ◽  
Alastair R. Hawkins ◽  
John R. Coggins ◽  
Chris Abell
Keyword(s):  
Substrate Specificity ◽  
Type I ◽  
Type Ii

CD95 ligation and intracellular membrane flow

2008 ◽  
Vol 413 (3) ◽  
pp. e11-e12 ◽  
Author(s):  
Roland Reinehr ◽  
Dieter Häussinger
Keyword(s):  
Plasma Membrane ◽  
Caspase 8 ◽  
Type I ◽  
Type Ii Cells ◽  
Type Ii ◽  
Intracellular Membrane ◽  
Membrane Flow ◽  
Type I Cells ◽  
Endosomal Acidification ◽  
I Cells

Whereas ligation of the CD95 death receptor in the plasma membrane of so-called type I cells leads to a direct caspase 8-dependent activation of downstream effector caspases, mitochondrial amplification of caspase 8-derived signals is required in so-called type II cells in order to execute apoptotic cell death. In type I cells CD95L (CD95 ligand) binding to CD95 results in a ceramide-dependent formation of the DISC (death-inducing signalling complex) and caspase 8-dependent CD95 clustering in the plasma membrane, followed by an internalization of these multimeric-receptor–DISC complexes. In contrast, in the hepatocyte, a type II cell, the bulk of CD95 is stored intracellularly under resting conditions and only a few ‘sentinel’ CD95 receptors are present in the plasma membrane. However, their activation by CD95L is sufficient to trigger a caspase 8-dependent endosomal acidification and a ceramide-dependent trafficking of intracellularly stored CD95 to the plasma membrane, thereby amplifying CD95 activation. Thus, in both type I and type II cells, ceramide and CD95 receptor endo- and exo-cytosis are involved in CD95-mediated apoptosis, but apparently in different ways. This, however, is not the only effect of CD95 ligation on intracellular membrane flow in type II cells, and evidence has been presented that soon after CD95 ligation Golgi elements intermix caspase-dependently with mitochondria. In this issue of the Biochemical Journal, Matarrese et al. report another aspect on endocytosis in response to CD95 ligation in type II cells, namely a caspase-independent endocytosis with vesicle translocation to the mitochondrial compartment, suggestive of an interplay between both organelles in the sense of an ‘organelle scrambling’. Thus early effects of CD95 activation on intracellular membrane flow may be much more complex than previously thought, but much has still to be learned about signalling mechanisms and the role they play in apoptosis.

scholarly journals Mechanism of substrate specificity of phosphatidylinositol phosphate kinases

2016 ◽  
Vol 113 (31) ◽  
pp. 8711-8716 ◽  
Author(s):  
Yagmur Muftuoglu ◽  
Yi Xue ◽  
Xiang Gao ◽  
Dianqing Wu ◽  
Ya Ha
Keyword(s):  
Substrate Specificity ◽  
Membrane Trafficking ◽  
Eukaryotic Cell ◽  
Crystallographic Analysis ◽  
Structural Motif ◽  
Type I ◽  
Phosphate Binding ◽  
Phosphatidylinositol Phosphate ◽  
Phosphatidylinositol 4 ◽  
Phosphatidylinositol 3

The phosphatidylinositol phosphate kinase (PIPK) family of enzymes is primarily responsible for converting singly phosphorylated phosphatidylinositol derivatives to phosphatidylinositol bisphosphates. As such, these kinases are central to many signaling and membrane trafficking processes in the eukaryotic cell. The three types of phosphatidylinositol phosphate kinases are homologous in sequence but differ in catalytic activities and biological functions. Type I and type II kinases generate phosphatidylinositol 4,5-bisphosphate from phosphatidylinositol 4-phosphate and phosphatidylinositol 5-phosphate, respectively, whereas the type III kinase produces phosphatidylinositol 3,5-bisphosphate from phosphatidylinositol 3-phosphate. Based on crystallographic analysis of the zebrafish type I kinase PIP5Kα, we identified a structural motif unique to the kinase family that serves to recognize the monophosphate on the substrate. Our data indicate that the complex pattern of substrate recognition and phosphorylation results from the interplay between the monophosphate binding site and the specificity loop: the specificity loop functions to recognize different orientations of the inositol ring, whereas residues flanking the phosphate binding Arg244 determine whether phosphatidylinositol 3-phosphate is exclusively bound and phosphorylated at the 5-position. This work provides a thorough picture of how PIPKs achieve their exquisite substrate specificity.

scholarly journals Type IIα phosphatidylinositol phosphate kinase associates with the plasma membrane via interaction with type I isoforms

2002 ◽  
Vol 363 (3) ◽  
pp. 563 ◽  
Author(s):  
Katherine A. HINCHLIFFE ◽  
Maria Luisa GIUDICI ◽  
Andrew J. LETCHER ◽  
Robin F. IRVINE
Keyword(s):  
Plasma Membrane ◽  
Type I ◽  
Phosphatidylinositol Phosphate ◽  
Phosphatidylinositol Phosphate Kinase
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