scholarly journals Molecular Investigations of the Structure and Function of the Protein Phosphatase 1−Spinophilin−Inhibitor 2 Heterotrimeric Complex

Biochemistry ◽  
2011 ◽  
Vol 50 (7) ◽  
pp. 1238-1246 ◽  
Author(s):  
Barbara Dancheck ◽  
Michael J. Ragusa ◽  
Marc Allaire ◽  
Angus C. Nairn ◽  
Rebecca Page ◽  
...  
Keyword(s):  
Protein Phosphatase ◽  
Structure And Function ◽  
Protein Phosphatase 1 ◽  
And Function

scholarly journals Phosphorylation and dephosphorylation of Ser852 and Ser889 control the clustering, localization and function of PAR3

2020 ◽  
Vol 133 (22) ◽  
pp. jcs244830
Author(s):  
Kazunari Yamashita ◽  
Keiko Mizuno ◽  
Kana Furukawa ◽  
Hiroko Hirose ◽  
Natsuki Sakurai ◽  
...  
Keyword(s):  
Tight Junction ◽  
Protein Phosphatase ◽  
Phosphorylation Site ◽  
Protein Phosphatase 1 ◽  
Membrane Domain ◽  
Unique Role ◽  
Cellular Events ◽  
Local Clustering ◽  
And Function ◽  
Specific Membrane

ABSTRACTCell polarity is essential for various asymmetric cellular events, and the partitioning defective (PAR) protein PAR3 (encoded by PARD3 in mammals) plays a unique role as a cellular landmark to establish polarity. In epithelial cells, PAR3 localizes at the subapical border, such as the tight junction in vertebrates, and functions as an apical determinant. Although we know a great deal about the regulators of PAR3 localization, how PAR3 is concentrated and localized to a specific membrane domain remains an important question to be clarified. In this study, we demonstrate that ASPP2 (also known as TP53BP2), which controls PAR3 localization, links PAR3 and protein phosphatase 1 (PP1). The ASPP2–PP1 complex dephosphorylates a novel phosphorylation site, Ser852, of PAR3. Furthermore, Ser852- or Ser889-unphosphorylatable PAR3 mutants form protein clusters, and ectopically localize to the lateral membrane. Concomitance of clustering and ectopic localization suggests that PAR3 localization is a consequence of local clustering. We also demonstrate that unphosphorylatable forms of PAR3 exhibited a low molecular turnover and failed to coordinate rapid reconstruction of the tight junction, supporting that both the phosphorylated and dephosphorylated states are essential for the functional integrity of PAR3.

scholarly journals Structure and function of the co-chaperone protein phosphatase 5 in cancer

2020 ◽  
Vol 25 (3) ◽  
pp. 383-394 ◽  
Author(s):  
Rebecca A. Sager ◽  
Natela Dushukyan ◽  
Mark Woodford ◽  
Mehdi Mollapour
Keyword(s):  
Protein Phosphatase ◽  
Structure And Function ◽  
Protein Phosphatase 5 ◽  
Chaperone Protein ◽  
And Function

scholarly journals Protein phosphatase 1 regulates assembly and function of the β-catenin degradation complex

2007 ◽  
Vol 26 (6) ◽  
pp. 1511-1521 ◽  
Author(s):  
Wen Luo ◽  
Annita Peterson ◽  
Benjamin A Garcia ◽  
Gary Coombs ◽  
Bente Kofahl ◽  
...  
Keyword(s):  
Protein Phosphatase ◽  
Protein Phosphatase 1 ◽  
And Function

scholarly journals Degeneracy and Function of the Ubiquitous RVXF Motif That Mediates Binding to Protein Phosphatase-1

2003 ◽  
Vol 278 (21) ◽  
pp. 18817-18823 ◽  
Author(s):  
Paulina Wakula ◽  
Monique Beullens ◽  
Hugo Ceulemans ◽  
Willy Stalmans ◽  
Mathieu Bollen
Keyword(s):  
Protein Phosphatase ◽  
Protein Phosphatase 1 ◽  
And Function ◽  
Rvxf Motif

Biogenesis and activity regulation of protein phosphatase 1

2017 ◽  
Vol 45 (1) ◽  
pp. 89-99 ◽  
Author(s):  
Iris Verbinnen ◽  
Monica Ferreira ◽  
Mathieu Bollen
Keyword(s):  
Protein Phosphatase ◽  
Protein Phosphatase 1 ◽  
Interacting Proteins ◽  
Subcellular Targeting ◽  
Substantial Fraction ◽  
Short Linear Motifs ◽  
Specific Subset ◽  
Linear Motifs ◽  
And Function ◽  
And Control

Protein phosphatase 1 (PP1) is expressed in all eukaryotic cells and catalyzes a substantial fraction of phosphoserine/threonine dephosphorylation reactions. It forms stable complexes with PP1-interacting proteins (PIPs) that guide the phosphatase throughout its life cycle and control its fate and function. The diversity of PIPs is huge (≈200 in vertebrates), and most of them combine short linear motifs to form large and unique interaction interfaces with PP1. Many PIPs have separate domains for PP1 anchoring, PP1 regulation, substrate recruitment and subcellular targeting, which enable them to direct associated PP1 to a specific subset of substrates and mediate acute activity control. Hence, PP1 functions as the catalytic subunit of a large number of multimeric holoenzymes, each with its own subset of substrates and mechanism(s) of regulation.

Structure and function of neural networks in the retina

1988 ◽  
Vol 46 ◽  
pp. 26-27
Author(s):  
Peter Sterling
Keyword(s):  
Ganglion Cells ◽  
Three Dimensional ◽  
Structure And Function ◽  
Synaptic Connections ◽  
Visual Axis ◽  
One Dimensional ◽  
Cat Retina ◽  
Ultrathin Sections ◽  
And Function ◽  
Insight Into

The synaptic connections in cat retina that link photoreceptors to ganglion cells have been analyzed quantitatively. Our approach has been to prepare serial, ultrathin sections and photograph en montage at low magnification (˜2000X) in the electron microscope. Six series, 100-300 sections long, have been prepared over the last decade. They derive from different cats but always from the same region of retina, about one degree from the center of the visual axis. The material has been analyzed by reconstructing adjacent neurons in each array and then identifying systematically the synaptic connections between arrays. Most reconstructions were done manually by tracing the outlines of processes in successive sections onto acetate sheets aligned on a cartoonist's jig. The tracings were then digitized, stacked by computer, and printed with the hidden lines removed. The results have provided rather than the usual one-dimensional account of pathways, a three-dimensional account of circuits. From this has emerged insight into the functional architecture.

Osseointegration interface of calcified bone and endosseous implants

1992 ◽  
Vol 50 (2) ◽  
pp. 1096-1097
Author(s):  
K.E. Krizan ◽  
J.E. Laffoon ◽  
M.J. Buckley
Keyword(s):  
Structure And Function ◽  
Titanium Implants ◽  
En Bloc ◽  
Endosseous Implants ◽  
Ultrastructural Studies ◽  
The Past ◽  
Cacodylate Buffer ◽  
One Year ◽  
And Function

With increase use of tissue-integrated prostheses in recent years it is a goal to understand what is happening at the interface between haversion bone and bulk metal. This study uses electron microscopy (EM) techniques to establish parameters for osseointegration (structure and function between bone and nonload-carrying implants) in an animal model. In the past the interface has been evaluated extensively with light microscopy methods. Today researchers are using the EM for ultrastructural studies of the bone tissue and implant responses to an in vivo environment. Under general anesthesia nine adult mongrel dogs received three Brånemark (Nobelpharma) 3.75 × 7 mm titanium implants surgical placed in their left zygomatic arch. After a one year healing period the animals were injected with a routine bone marker (oxytetracycline), euthanized and perfused via aortic cannulation with 3% glutaraldehyde in 0.1M cacodylate buffer pH 7.2. Implants were retrieved en bloc, harvest radiographs made (Fig. 1), and routinely embedded in plastic. Tissue and implants were cut into 300 micron thick wafers, longitudinally to the implant with an Isomet saw and diamond wafering blade [Beuhler] until the center of the implant was reached.

Sign in / Sign up

Export Citation Format

Share Document