Silver-mediated direct C–H amination of BODIPYs for screening endoplasmic reticulum-targeting reagents

2018 ◽  
Vol 54 (26) ◽  
pp. 3219-3222 ◽  
Author(s):  
Huaxing Zhang ◽  
Xingyu Chen ◽  
Jingbo Lan ◽  
Yanhong Liu ◽  
Fulin Zhou ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Highly Efficient ◽  
Er Targeting ◽  
Endoplasmic Reticulum Targeting

A highly efficient Ag(i)-mediated direct C–H amination of BODIPYs is accomplished. BODIPYs 3q and 4b exhibit specific ER-targeting capacities.

scholarly journals Endoplasmic reticulum targeting fluorescent probes to image mobile Zn2+

2019 ◽  
Vol 10 (47) ◽  
pp. 10881-10887 ◽  
Author(s):  
Le Fang ◽  
Giuseppe Trigiante ◽  
Rachel Crespo-Otero ◽  
Chris S. Hawes ◽  
Michael P. Philpott ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Fluorescent Probes ◽  
Biological Processes ◽  
Er Targeting ◽  
Endoplasmic Reticulum Targeting

Two endoplasmic reticulum (ER) targeting probes were developed to image mobile Zn2+ to help understand Zn2+ related biological processes in the ER.

scholarly journals Autophagy requires endoplasmic reticulum targeting of the PI3-kinase complex via Atg14L

2010 ◽  
Vol 190 (4) ◽  
pp. 511-521 ◽  
Author(s):  
Kohichi Matsunaga ◽  
Eiji Morita ◽  
Tatsuya Saitoh ◽  
Shizuo Akira ◽  
Nicholas T. Ktistakis ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Mammalian Cells ◽  
Embryonic Stem ◽  
Pi3 Kinase ◽  
Class Iii ◽  
Autophagosome Formation ◽  
Membranous Structure ◽  
Er Targeting ◽  
Endoplasmic Reticulum Targeting ◽  
Phosphatidylinositol 3

Autophagy is a catabolic process that allows cells to digest their cytoplasmic constituents via autophagosome formation and lysosomal degradation. Recently, an autophagy-specific phosphatidylinositol 3-kinase (PI3-kinase) complex, consisting of hVps34, hVps15, Beclin-1, and Atg14L, has been identified in mammalian cells. Atg14L is specific to this autophagy complex and localizes to the endoplasmic reticulum (ER). Knockdown of Atg14L leads to the disappearance of the DFCP1-positive omegasome, which is a membranous structure closely associated with both the autophagosome and the ER. A point mutation in Atg14L resulting in defective ER localization was also defective in the induction of autophagy. The addition of the ER-targeting motif of DFCP1 to this mutant fully complemented the autophagic defect in Atg14L knockout embryonic stem cells. Thus, Atg14L recruits a subset of class III PI3-kinase to the ER, where otherwise phosphatidylinositol 3-phosphate (PI3P) is essentially absent. The Atg14L-dependent appearance of PI3P in the ER makes this organelle the platform for autophagosome formation.

An endoplasmic reticulum-targeting fluorescent probe for the imaging of GSH in living cells

2019 ◽  
Vol 11 (29) ◽  
pp. 3736-3740 ◽  
Author(s):  
Cheng-Shi Jiang ◽  
Zhi-Qiang Cheng ◽  
Yong-Xi Ge ◽  
Jia-Li Song ◽  
Juan Zhang ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Fluorescent Probe ◽  
Living Cells ◽  
Er Targeting ◽  
Endoplasmic Reticulum Targeting

A new endoplasmic reticulum (ER)-targeting fluorescent probe (ER-G) was designed and applied for the detection of cellular GSH in the ER.

The development of an endoplasmic reticulum-targeting fluorescent probe for the imaging of 1,4-dithiothreitol (DTT) in living cells

2021 ◽  
Author(s):  
Abdul Hadi Mehmood ◽  
Baoli Dong ◽  
Yaru Lu ◽  
Wenhui Song ◽  
Yaru Sun ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Fluorescent Probe ◽  
Living Cells ◽  
Turn On ◽  
Er Targeting ◽  
Endoplasmic Reticulum Targeting ◽  
First Time

An effective turn-on ER-targeting fluorescent probe ER-DTT was designed to image DTT of endoplasmic reticulum for the first time.

An endoplasmic reticulum-targeting fluorescent probe for imaging ˙OH in living cells

2020 ◽  
Vol 56 (47) ◽  
pp. 6344-6347 ◽  
Author(s):  
Yanyan Zhao ◽  
Hongyu Li ◽  
Ziyin Chai ◽  
Wen Shi ◽  
Xiaohua Li ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Er Stress ◽  
Fluorescent Probe ◽  
Lipid Droplet ◽  
Droplet Formation ◽  
Living Cells ◽  
Lipid Droplet Formation ◽  
Er Targeting ◽  
Endoplasmic Reticulum Targeting

A new ER-targeting fluorescent probe for ˙OH is developed and applied to imaging ˙OH generation as well as lipid droplet formation in ER stress.

Cell-penetrating peptide-conjugated lipid/polymer hybrid nanovesicles for endoplasmic reticulum-targeting intracellular delivery

2021 ◽  
Author(s):  
Jeong Yi Kang ◽  
Seulgi Kim ◽  
Juhyeon Kim ◽  
Nae-Gyu Kang ◽  
Chul-Su Yang ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Intracellular Delivery ◽  
Cell Penetrating Peptide ◽  
Polymer Hybrid ◽  
Cell Penetrating ◽  
Er Targeting ◽  
Endoplasmic Reticulum Targeting ◽  
Delivery Approach

An ER-targeting, intracellular delivery approach that utilizes cell-penetrating peptide-conjugated lipid/polymer hybrid nanovehicles is proposed.

scholarly journals Membrane Topogenesis of a Type I Signal-Anchor Protein, Mouse Synaptotagmin Ii, on the Endoplasmic Reticulum

2000 ◽  
Vol 150 (4) ◽  
pp. 719-730 ◽  
Author(s):  
Yuichiro Kida ◽  
Masao Sakaguchi ◽  
Mitsunori Fukuda ◽  
Katsuhiko Mikoshiba ◽  
Katsuyoshi Mihara
Keyword(s):  
Endoplasmic Reticulum ◽  
Endoplasmic Reticulum Membrane ◽  
Type I ◽  
Hydrophobic Region ◽  
Anchor Protein ◽  
Nascent Polypeptide ◽  
Charged Residues ◽  
Er Targeting ◽  
Signal Anchor ◽  
Positively Charged

Synaptotagmin II is a type I signal-anchor protein, in which the NH2-terminal domain of 60 residues (N-domain) is located within the lumenal space of the membrane and the following hydrophobic region (H-region) shows transmembrane topology. We explored the early steps of cotranslational integration of this molecule on the endoplasmic reticulum membrane and demonstrated the following: (a) The translocation of the N-domain occurs immediately after the H-region and the successive positively charged residues emerge from the ribosome. (b) Positively charged residues that follow the H-region are essential for maintaining the correct topology. (c) It is possible to dissect the lengths of the nascent polypeptide chains which are required for ER targeting of the ribosome and for translocation of the N-domain, thereby demonstrating that different nascent polypeptide chain lengths are required for membrane targeting and N-domain translocation. (d) The H-region is sufficiently long for membrane integration. (e) Proline residues preceding H-region are critical for N-domain translocation, but not for ER targeting. The proline can be replaced with amino acid with low helical propensity.

scholarly journals A Retention Signal Necessary and Sufficient for Endoplasmic Reticulum Localization Maps to the Transmembrane Domain of Hepatitis C Virus Glycoprotein E2

1998 ◽  
Vol 72 (3) ◽  
pp. 2183-2191 ◽  
Author(s):  
Laurence Cocquerel ◽  
Jean-Christophe Meunier ◽  
André Pillez ◽  
Czeslaw Wychowski ◽  
Jean Dubuisson
Keyword(s):  
Endoplasmic Reticulum ◽  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Transmembrane Domain ◽  
Intracellular Localization ◽  
Native Form ◽  
Glycosyl Phosphatidylinositol ◽  
Er Retention ◽  
Er Targeting ◽  
Necessary And Sufficient

ABSTRACT The hepatitis C virus (HCV) genome encodes two envelope glycoproteins (E1 and E2). These glycoproteins interact to form a noncovalent heterodimeric complex which is retained in the endoplasmic reticulum (ER). To identify whether E1 and/or E2 contains an ER-targeting signal potentially involved in ER retention of the E1-E2 complex, these proteins were expressed alone and their intracellular localization was studied. Due to misfolding of E1 in the absence of E2, no conclusion on the localization of its native form could be drawn from the expression of E1 alone. E2 expressed in the absence of E1 was shown to be retained in the ER similarly to E1-E2 complex. Chimeric proteins in which E2 domains were exchanged with corresponding domains of a protein normally transported to the plasma membrane (CD4) were constructed to identify the sequence responsible for its ER retention. The transmembrane domain (TMD) of E2 (C-terminal 29 amino acids) was shown to be sufficient for retention of the ectodomain of CD4 in the ER compartment. Replacement of the E2 TMD by the anchor signal of CD4 or a glycosyl phosphatidylinositol (GPI) moiety led to its expression on the cell surface. In addition, replacement of the E2 TMD by the anchor signal of CD4 or a GPI moiety abolished the formation of E1-E2 complexes. Together, these results suggest that, besides having a role as a membrane anchor, the TMD of E2 is involved in both complex formation and intracellular localization.

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