scholarly journals Cytoskeleton-Associated Protein 4: Functions Beyond the Endoplasmic Reticulum in Physiology and Disease

2012 ◽  
Vol 2012 ◽  
pp. 1-11 ◽  
Author(s):  
Kevin M. Tuffy ◽  
Sonia Lobo Planey
Keyword(s):  
Endoplasmic Reticulum ◽  
Cell Types ◽  
Lipid Homeostasis ◽  
Drug Induced ◽  
Microtubule Network ◽  
Major Function ◽  
Lung Lipid ◽  
Intermediate Compartment ◽  
Rough Er ◽  
Cellular Compartments

Cytoskeleton-associated protein 4 (CKAP4; also known as p63, CLIMP-63, or ERGIC-63) is a 63 kDa, reversibly palmitoylated and phosphorylated, type II transmembrane (TM) protein, originally identified as a resident of the endoplasmic reticulum (ER)/Golgi intermediate compartment (ERGIC). When localized to the ER, a major function of CKAP4 is to anchor rough ER to microtubules, organizing the overall structure of ER with respect to the microtubule network. There is also steadily accumulating evidence for diverse roles for CKAP4 localized outside the ER, including data demonstrating functionality of cell surface forms of CKAP4 in various cell types and of CKAP4 in the nucleus. We will review the recent studies that provide evidence for the existence of CKAP4 in multiple cellular compartments (i.e., ER, plasma membrane, and the nucleus) and discuss CKAP4’s role in the regulation of various physiological and pathological processes, such as interstitial cystitis, drug-induced cytotoxicity, pericullar proteolytic activity, and lung lipid homeostasis.

scholarly journals Syntaxin 17 Is Abundant in Steroidogenic Cells and Implicated in Smooth Endoplasmic Reticulum Membrane Dynamics

2000 ◽  
Vol 11 (8) ◽  
pp. 2719-2731 ◽  
Author(s):  
Martin Steegmaier ◽  
Viola Oorschot ◽  
Judith Klumperman ◽  
Richard H. Scheller
Keyword(s):  
Endoplasmic Reticulum ◽  
Smooth Endoplasmic Reticulum ◽  
Regulatory Protein ◽  
Cell Types ◽  
Membrane Dynamics ◽  
Endoplasmic Reticulum Membrane ◽  
Steroidogenic Cell ◽  
Molecular Machinery ◽  
Intermediate Compartment ◽  
Steroidogenic Cells

The endoplasmic reticulum (ER) consists of subcompartments that have distinct protein constituents, morphological appearances, and functions. To understand the mechanisms that regulate the intricate and dynamic organization of the endoplasmic reticulum, it is important to identify and characterize the molecular machinery involved in the assembly and maintenance of the different subcompartments. Here we report that syntaxin 17 is abundantly expressed in steroidogenic cell types and specifically localizes to smooth membranes of the ER. By immunoprecipitation analyses, syntaxin 17 exists in complexes with a syntaxin regulatory protein, rsly1, and/or two intermediate compartment SNARE proteins, rsec22b and rbet1. Furthermore, we found that syntaxin 17 is anchored to the smooth endoplasmic reticulum through an unusual mechanism, requiring two adjacent hydrophobic domains near its carboxyl terminus. Converging lines of evidence indicate that syntaxin 17 functions in a vesicle-trafficking step to the smooth-surfaced tubular ER membranes that are abundant in steroidogenic cells.

scholarly journals NUCLEOSIDE DIPHOSPHATASE AND THIAMINE PYROPHOSPHATASE ACTIVITIES IN THE ENDOPLASMIC RETICULUM AND GOLGI APPARATUS

1971 ◽  
Vol 19 (6) ◽  
pp. 349-360 ◽  
Author(s):  
SIDNEY GOLDFISCHER ◽  
BERNICE SCHILLER ◽  
EDWARD ESSNER
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Cell Types ◽  
Thiamine Pyrophosphatase ◽  
Single Protein ◽  
Effects Of Ph ◽  
Rough Er ◽  
Neonatal Hepatocytes ◽  
Multiple Configurations ◽  
Nucleoside Diphosphatase

The effects of pH, fixatives and divalent ions on nucleoside diphosphatase (NDPase) and thiamine pyrophosphatase (TPPase) activities in the endoplasmic reticulum (ER) and Golgi apparatus (GA) were examined in adult and neonatal hepatocytes and other cell types in the rat. In liver cells TPPase and NDPase both have a similar localization in the rough ER, nuclear envelope and smooth ER but differ in their pH optima; TPPase is most active at pH 8, NDPase at pH 7. TPPase in the GA, unlike its counterpart in the ER, is most active at neutral pH. High levels of NDPase activity are present in the GA of neurons, epididymis and other cells, but not in hepatocytes. TPPase in the ER, but not the GA, is stimulated by the addition of adenosine triphosphate to the medium. These observations show that different conditions are required to demonstrate ER and GA diphosphatase activities. Whether separate enzymes or multiple configurations of a single protein are responsible for these activities cannot be determined by staining procedures.

scholarly journals The isolated ER-Golgi intermediate compartment exhibits properties that are different from ER and cis-Golgi.

1991 ◽  
Vol 113 (1) ◽  
pp. 45-54 ◽  
Author(s):  
A Schweizer ◽  
K Matter ◽  
C M Ketcham ◽  
H P Hauri
Keyword(s):  
Protein Transport ◽  
Gradient Centrifugation ◽  
Cell Types ◽  
Vero Cells ◽  
Subcellular Fractionation ◽  
Fractionation Procedure ◽  
Targeting Signal ◽  
Intermediate Compartment ◽  
Rough Er ◽  
Protein Disulfide

A procedure has been established in Vero cells for the isolation of an intermediate compartment involved in protein transport from the ER to the Golgi apparatus. The two-step subcellular fractionation procedure consists of Percoll followed by Metrizamide gradient centrifugation. Using the previously characterized p53 as a marker protein, the average enrichment factor of the intermediate compartment was 41. The purified fraction displayed a unique polypeptide pattern. It was largely separated from the rough ER proteins ribophorin I, ribophorin II, BIP, and protein disulfide isomerase, as well as from the putative cis-Golgi marker N-acetylglucosamine-1-phosphodiester-alpha-N-acetylglucosaminidase, the second of the two enzymes generating the lysosomal targeting signal mannose-6-phosphate. The first enzyme, N-acetylglucosaminylphosphotransferase, for which previous biochemical evidence had suggested both a pre- and a cis-Golgi localization in other cell types, cofractionated with the cis-Golgi rather than the intermediate compartment in Vero cells. The results suggest that the intermediate compartment defined by p53 has unique properties and does not exhibit typical features of rough ER and cis-Golgi.

In Vitro Induction of Crystals of MT Protein by Vinblastine-Colcemid in Mouse Spermatids

1974 ◽  
Vol 32 ◽  
pp. 132-133
Author(s):  
John J. Wolosewick ◽  
John H. D. Bryan
Keyword(s):  
Endoplasmic Reticulum ◽  
Smooth Endoplasmic Reticulum ◽  
Nuclear Ring ◽  
Rough Er ◽  
Distal Direction ◽  
In Vitro Induction

Early in spermiogenesis the manchette is rapidly assembled in a distal direction from the nuclear-ring-densities. The association of vesicles of smooth endoplasmic reticulum (SER) and the manchette microtubules (MTS) has been reported. In the mouse, osmophilic densities at the distal ends of the manchette are the organizing centers (MTOCS), and are associated with the SER. Rapid MT assembly and the lack of rough ER suggests that there is an existing pool of MT protein. Colcemid potentiates the reaction of vinblastine with tubulin and was used in this investigation to detect this protein.

Prevalence of the pit and antipit in the genus Glycine

1987 ◽  
Vol 45 ◽  
pp. 986-987
Author(s):  
R. W. Yaklich ◽  
E. L. Vigil ◽  
W. P. Wergin
Keyword(s):  
Amino Acids ◽  
Endoplasmic Reticulum ◽  
Glycine Max ◽  
Seed Coat ◽  
Cell Types ◽  
Abaxial Surface ◽  
Legume Seed ◽  
Initial Report ◽  
Cone Cells ◽  
Glycine Max L

The legume seed coat is the site of sucrose unloading and the metabolism of imported ureides and synthesis of amino acids for the developing embryo. The cell types directly responsible for these functions in the seed coat are not known. We recently described a convex layer of tissue on the inside surface of the soybean (Glycine max L. Merr.) seed coat that was termed “antipit” because it was in direct opposition to the concave pit on the abaxial surface of the cotyledon. Cone cells of the antipit contained numerous hypertrophied Golgi apparatus and laminated rough endoplasmic reticulum common to actively secreting cells. The initial report by Dzikowski (1936) described the morphology of the pit and antipit in G. max and found these structures in only 68 of the 169 seed accessions examined.

scholarly journals Mitochondria-rough-ER contacts in the liver regulate systemic lipid homeostasis

Cell Reports ◽  
2021 ◽  
Vol 34 (11) ◽  
pp. 108873
Author(s):  
Irene Anastasia ◽  
Nicolò Ilacqua ◽  
Andrea Raimondi ◽  
Philippe Lemieux ◽  
Rana Ghandehari-Alavijeh ◽  
...  
Keyword(s):  
Lipid Homeostasis ◽  
Rough Er

scholarly journals Single cell transcriptomic analysis of murine lung development on hyperoxia-induced damage

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Maria Hurskainen ◽  
Ivana Mižíková ◽  
David P. Cook ◽  
Noora Andersson ◽  
Chanèle Cyr-Depauw ◽  
...  
Keyword(s):  
Single Cell ◽  
Lung Development ◽  
Alveolar Epithelium ◽  
Cell Types ◽  
Capillary Endothelium ◽  
Stromal Fibroblasts ◽  
Main Driver ◽  
Macrophage Populations ◽  
Induced Changes ◽  
Cellular Compartments

AbstractDuring late lung development, alveolar and microvascular development is finalized to enable sufficient gas exchange. Impaired late lung development manifests as bronchopulmonary dysplasia (BPD) in preterm infants. Single-cell RNA sequencing (scRNA-seq) allows for assessment of complex cellular dynamics during biological processes, such as development. Here, we use MULTI-seq to generate scRNA-seq profiles of over 66,000 cells from 36 mice during normal or impaired lung development secondary to hyperoxia with validation of some of the findings in lungs from BPD patients. We observe dynamic populations of cells, including several rare cell types and putative progenitors. Hyperoxia exposure, which mimics the BPD phenotype, alters the composition of all cellular compartments, particularly alveolar epithelium, stromal fibroblasts, capillary endothelium and macrophage populations. Pathway analysis and predicted dynamic cellular crosstalk suggest inflammatory signaling as the main driver of hyperoxia-induced changes. Our data provides a single-cell view of cellular changes associated with late lung development in health and disease.

scholarly journals Effects of taurolithocholate, a Ca2+-mobilizing agent, on cell Ca2+ in rat hepatocytes, human platelets and neuroblastoma NG108-15 cell line

1991 ◽  
Vol 273 (1) ◽  
pp. 153-160 ◽  
Author(s):  
J F Coquil ◽  
B Berthon ◽  
N Chomiki ◽  
L Combettes ◽  
P Jourdon ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Bile Acid ◽  
Cell Line ◽  
Rat Liver ◽  
Neuronal Cell ◽  
Rat Hepatocytes ◽  
Cell Types ◽  
Liver Cells ◽  
Human Platelets ◽  
Rat Liver Cells

The monohydroxy bile acid taurolithocholate permeabilizes the endoplasmic reticulum to Ca2+ in rat liver cells. To assess whether this action on the endoplasmic reticulum was restricted to this tissue, the effects of bile acid were investigated in two cell types quite unrelated to rat hepatocyte, namely human platelets and neuronal NG108-15 cell line. The results showed that taurolithocholate (3-100 microM) had no effect on free cytosolic [Ca2+] in human platelets and NG108-15 cells. whereas it increased it from 180 to 520 nM in rat hepatocytes. In contrast, in cells permeabilized by saponin, taurolithocholate initiated a profound release of the stored Ca2+ from the internal Ca2+ pools in the three cell types. The bile acid released 90% of the Ca2+ pools, with rate constants of about 5 min-1 and half-maximal effects at 15-30 microM. The results also showed that, in contrast with liver cells, which displayed an influx of [14C]taurolithocholate of 2 nmol/min per mg, human platelets and the neuronal cell line appeared to be resistant to [14C]taurolithocholate uptake. The influx measured in these latter cells was about 100-fold lower than in rat liver cells. Taken together, these data suggest that human platelets and NG108-15 cells do not possess the transport system for concentrating monohydroxy bile acids into cells. However, they show that human platelets and neuronal NG108-15 possess, in common with liver cells, the intracellular system responsible for taurolithocholate-mediated Ca2+ release from internal stores.

Selective Accumulation of the Endoplasmic Reticulum–Golgi Intermediate Compartment Induced by the Antitumor Drug KRN5500

2000 ◽  
Vol 256 (2) ◽  
pp. 468-479 ◽  
Author(s):  
Masaru Kamishohara ◽  
Susan Kenney ◽  
Renee Domergue ◽  
David T. Vistica ◽  
Edward A. Sausville
Keyword(s):  
Endoplasmic Reticulum ◽  
Antitumor Drug ◽  
Intermediate Compartment ◽  
Selective Accumulation
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