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 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

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.

Initiation of HeLa cell adhesion to collagen is dependent upon collagen receptor upregulation, segregation to the basal plasma membrane, clustering and binding to the cytoskeleton

1992 ◽  
Vol 101 (4) ◽  
pp. 873-883
Author(s):  
M.L. Lu ◽  
R.J. McCarron ◽  
B.S. Jacobson
Keyword(s):  
Plasma Membrane ◽  
Cell Attachment ◽  
Cell Spreading ◽  
Threshold Effect ◽  
Type I ◽  
Receptor Clustering ◽  
Collagen Receptors ◽  
Basal Plasma Membrane ◽  
Basal Plasma ◽  
Collagen Receptor

It was recently reported that HeLa cells have three Arg-Gly-Asp-dependent collagen receptors that do not appear to be in the integrin family of extracellular matrix receptors and bind to either type I or IV collagen or to type I gelatin. It was our goal to determine how these receptors function in HeLa cell-substratum adhesion. We report here that the sequence of events by which the receptors mediate adhesion to collagen or gelatin is: (1) induction of cell attachment by specific collagen receptor-substratum interactions with culture dishes covalently coated with either type I collagen or gelatin - attachment is inhibited by soluble gelatin; (2) stabilization of attachment by exocytotic upregulation of the receptors to the basal plasma membrane, which was demonstrated by analyzing, during cell adhesion, the redistribution of the collagen receptors among the apical plasma membrane exposed to the culture medium, the basal plasma membrane contacting the culture dish, and an intracellular pool of plasma membrane vesicles; (3) the initiation of cell spreading by receptor clustering and cytoskeletal association. Cell spreading is a threshold effect with regard to the surface concentration of gelatin, indicating that collagen receptor clustering is a precondition to the onset of spreading. Observations consistent with this interpretation of the threshold effect are that cells attach but spread more slowly on a substratum that retards receptor clustering, and that collagen receptors, when viewed by immunofluorescence microscopy, form a punctate pattern of fluorescence in the basal plasma membrane during cell spreading. It is also shown that more collagen receptors co-isolate with nondenaturing detergent-stable cytoskeletal preparations after the collagen receptors have been either clustered by antibodies or gelatin in solution, or by a collagen matrix. This indicates that clustering drives the receptors to bind to the cytoskeleton and is a necessary step in the transition from cell attachment to cell spreading.

Exercise increases the plasma membrane content of the Na+ -K+ pump and its mRNA in rat skeletal muscles

1996 ◽  
Vol 80 (2) ◽  
pp. 699-705 ◽  
Author(s):  
T. Tsakiridis ◽  
P. P. Wong ◽  
Z. Liu ◽  
C. D. Rodgers ◽  
M. Vranic ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Plasma Membrane ◽  
Skeletal Muscles ◽  
Plasma Membranes ◽  
Acute Exercise ◽  
Treadmill Running ◽  
Type I ◽  
Mrna Levels ◽  
Subunit Mrna ◽  
White Type

Muscle fibers adapt to ionic challenges of exercise by increasing the plasma membrane Na+-K+ pump activity. Chronic exercise training has been shown to increase the total amount of Na+-K+ pumps present in skeletal muscle. However, the mechanism of adaptation of the Na+-K+ pump to an acute bout of exercise has not been determined, and it is not known whether it involves alterations in the content of plasma membrane pump subunits. Here we examine the effect of 1 h of treadmill running (20 m/min, 10% grade) on the subcellular distribution and expression of Na+-K+ pump subunits in rat skeletal muscles. Red type I and IIa (red-I/IIa) and white type IIa and IIb (white-IIa/IIb) hindlimb muscles from resting and exercised female Sprague-Dawley rats were removed for subcellular fractionation. By homogenization and gradient centrifugation, crude membranes and purified plasma membranes were isolated and subjected to gel electrophoresis and immunoblotting by using pump subunit-specific antibodies. Furthermore, mRNA was isolated from specific red type I (red-I) and white type IIb (white-IIb) muscles and subjected to Northern blotting by using subunit-specific probes. In both red-I/IIa and white-IIa/IIb muscles, exercise significantly raised the plasma membrane content of the alpha1-subunit of the pump by 64 +/- 24 and 55 +/- 22%, respectively (P < 0.05), and elevated the alpha2-polypeptide by 43 +/- 22 and 94 +/- 39%, respectively (P < 0.05). No significant effect of exercise could be detected on the amount of these subunits in an internal membrane fraction or in total membranes. In addition, exercise significantly increased the alpha1-subunit mRNA in red-I muscle (by 50 +/- 7%; P < 0.05) and the beta2-subunit mRNA in white-IIb muscles (by 64 +/- 19%; P < 0.01), but the alpha2- and beta1-mRNA levels were unaffected in this time period. We conclude that increased presence of alpha1- and alpha2-polypeptides at the plasma membrane and subsequent elevation of the alpha1- and beta2-subunit mRNAs may be mechanisms by which acute exercise regulates the Na+-K+ pump of skeletal muscle.

scholarly journals Live cell micropatterning reveals the dynamics of signaling complexes at the plasma membrane

2014 ◽  
Vol 207 (3) ◽  
pp. 407-418 ◽  
Author(s):  
Sara Löchte ◽  
Sharon Waichman ◽  
Oliver Beutel ◽  
Changjiang You ◽  
Jacob Piehler
Keyword(s):  
Plasma Membrane ◽  
Single Molecule ◽  
Spatial Organization ◽  
Polymer Brush ◽  
Effector Proteins ◽  
Live Cells ◽  
Type I ◽  
Rgd Peptides ◽  
Single Molecule Level ◽  
Cell Micropatterning

Interactions of proteins in the plasma membrane are notoriously challenging to study under physiological conditions. We report in this paper a generic approach for spatial organization of plasma membrane proteins into micropatterns as a tool for visualizing and quantifying interactions with extracellular, intracellular, and transmembrane proteins in live cells. Based on a protein-repellent poly(ethylene glycol) polymer brush, micropatterned surface functionalization with the HaloTag ligand for capturing HaloTag fusion proteins and RGD peptides promoting cell adhesion was devised. Efficient micropatterning of the type I interferon (IFN) receptor subunit IFNAR2 fused to the HaloTag was achieved, and highly specific IFN binding to the receptor was detected. The dynamics of this interaction could be quantified on the single molecule level, and IFN-induced receptor dimerization in micropatterns could be monitored. Assembly of active signaling complexes was confirmed by immunostaining of phosphorylated Janus family kinases, and the interaction dynamics of cytosolic effector proteins recruited to the receptor complex were unambiguously quantified by fluorescence recovery after photobleaching.

Internalisation of the type I angiotensin II receptor (ATI) and angiotensin II function in the rat adrenal zona glomerulosa cell.

1994 ◽  
Vol 141 (2) ◽  
pp. R5-R9 ◽  
Author(s):  
G. P. Vinson ◽  
M. M. Ho. ◽  
J.R. Puddefoot ◽  
R. Teja ◽  
S. Barker
Keyword(s):  
Monoclonal Antibody ◽  
Plasma Membrane ◽  
Angiotensin Ii ◽  
Zona Glomerulosa ◽  
Type I ◽  
Specific Monoclonal Antibody ◽  
Angiotensin Ii Receptor ◽  
Cellular Localisation ◽  
Glomerulosa Cells

ABSTRACT Little is known about the cellular localisation of the angiotensin II (AII) type 1 receptor (ATI) in the rat adrenal glomerulosa cell, but some studies have suggested that receptor internalisation and recycling may occur. Using a specific monoclonal antibody (6313/G2) to the first extracellular domain, we show here that most of the receptor is internalised in the unstimulated cell. When viable glomerulosa cells are incubated with 6313/G2, the receptor is transiently concentrated on the cell surface, and aldosterone output is stimulated. This stimulated output is enhanced by neither threshold nor maximal stimulatory concentrations of All amide, although the antibody does not inhibit All binding to the receptor. Conversely, the stimulatory actions of the antibody and those of ACTH are additive. The data suggest that recycling to the plasma membrane is constitutive, or regulated by unknown factors. Retention of the ATI receptor in the membrane is alone enough to allow sufficient G protein interaction to generate maximal stimulatory events.

scholarly journals Exocytosis of Alphaherpesvirus Virions, Light Particles, and Glycoproteins Uses Constitutive Secretory Mechanisms

mBio ◽  
2016 ◽  
Vol 7 (3) ◽  
Author(s):  
Ian B. Hogue ◽  
Julian Scherer ◽  
Lynn W. Enquist
Keyword(s):  
Plasma Membrane ◽  
Virus Particle ◽  
Immune Evasion ◽  
Host Cells ◽  
Type I ◽  
Rab Gtpases ◽  
Viral Glycoprotein ◽  
Particle Assembly ◽  
Viral Glycoproteins ◽  
Light Particles

ABSTRACTMany molecular and cell biological details of the alphaherpesvirus assembly and egress pathway remain unclear. Recently we developed a live-cell fluorescence microscopy assay of pseudorabies virus (PRV) exocytosis, based ontotalinternalreflectionfluorescence (TIRF) microscopy and a virus-encoded pH-sensitive fluorescent probe. Here, we use this assay to distinguish three classes of viral exocytosis in a nonpolarized cell type: (i) trafficking of viral glycoproteins to the plasma membrane, (ii) exocytosis of viral light particles, and (iii) exocytosis of virions. We find that viral glycoproteins traffic to the cell surface in association with constitutive secretory Rab GTPases and exhibit free diffusion into the plasma membrane after exocytosis. Similarly, both virions and light particles use these same constitutive secretory mechanisms for egress from infected cells. Furthermore, we show that viral light particles are distinct from cellular exosomes. Together, these observations shed light on viral glycoprotein trafficking steps that precede virus particle assembly and reinforce the idea that virions and light particles share a biogenesis and trafficking pathway.IMPORTANCEThe alphaherpesviruses, including the important human pathogens herpes simplex virus 1 (HSV-1), HSV-2, and varicella-zoster virus (VZV), are among the few viruses that have evolved to exploit the mammalian nervous system. These viruses typically cause mild recurrent herpetic or zosteriform lesions but can also cause debilitating herpes encephalitis, more frequently in very young, old, immunocompromised, or nonnatural hosts. Importantly, many of the molecular and cellular mechanisms of viral assembly and egress remain unclear. This study addresses the trafficking of viral glycoproteins to the plasma membrane, exocytosis of light particles, and exocytosis of virions. Trafficking of glycoproteins affects immune evasion and pathogenesis and may precede virus particle assembly. The release of light particles may also contribute to immune evasion and pathogenesis. Finally, exocytosis of virions is important to understand, as this final step in the virus replication cycle produces infectious extracellular particles capable of spreading to the next round of host cells.

Sign in / Sign up

Export Citation Format

Share Document