scholarly journals An Orchestrated Program Regulating Secretory Pathway Genes and Cargos by the Transmembrane Transcription Factor CREB-H

Traffic ◽  
2013 ◽  
Vol 14 (4) ◽  
pp. 382-398 ◽  
Author(s):  
Sónia Barbosa ◽  
Giovanna Fasanella ◽  
Suzanne Carreira ◽  
Marta Llarena ◽  
Rebecca Fox ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Secretory Pathway

scholarly journals The C2H2 Transcription Factor REGULATOR OF SYMBIOSOME DIFFERENTIATION Represses Transcription of the Secretory Pathway Gene VAMP721a and Promotes Symbiosome Development in Medicago truncatula

2013 ◽  
Vol 25 (9) ◽  
pp. 3584-3601 ◽  
Author(s):  
Senjuti Sinharoy ◽  
Ivone Torres-Jerez ◽  
Kaustav Bandyopadhyay ◽  
Attila Kereszt ◽  
Catalina I. Pislariu ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Medicago Truncatula ◽  
Secretory Pathway ◽  
Pathway Gene

scholarly journals Mesenchymal-to-epithelial transitions require tissue-specific interactions with distinct laminins

2021 ◽  
Vol 220 (8) ◽  
Author(s):  
Ioanna Pitsidianaki ◽  
Jason Morgan ◽  
Jamie Adams ◽  
Kyra Campbell
Keyword(s):  
Transcription Factor ◽  
Drosophila Melanogaster ◽  
Secretory Pathway ◽  
Columnar Epithelium ◽  
Specific Interactions ◽  
Down Regulation ◽  
Α Subunit ◽  
Tissue Specific ◽  
Mesenchymal To Epithelial Transition

Mesenchymal-to-epithelial transition (MET) converts cells from migratory mesenchymal to polarized epithelial states. Despite its importance for both normal and pathological processes, very little is known about the regulation of MET in vivo. Here we exploit midgut morphogenesis in Drosophila melanogaster to investigate the mechanisms underlying MET. We show that down-regulation of the EMT transcription factor Serpent is required for MET, but not sufficient, as interactions with the surrounding mesoderm are also essential. We find that midgut MET relies on the secretion of specific laminins via the CopII secretory pathway from both mesoderm and midgut cells. We show that secretion of the laminin trimer containing the Wingblister α-subunit from the mesoderm is an upstream cue for midgut MET, leading to basal polarization of αPS1 integrin in midgut cells. Polarized αPS1 is required for the formation of a monolayered columnar epithelium and for the apical polarization of αPS3, Baz, and E-Cad. Secretion of a distinct LamininA-containing trimer from midgut cells is required to reinforce the localization of αPS1 basally, and αPS3 apically, for robust repolarization. Our data suggest that targeting these MET pathways, in conjunction with therapies preventing EMT, may present a two-pronged strategy toward blocking metastasis in cancer.

scholarly journals Regulation of human prohormone convertase 2 promoter activity by the transcription factor EGR-1

1997 ◽  
Vol 328 (1) ◽  
pp. 69-74 ◽  
Author(s):  
Erik JANSEN ◽  
A. Y. Torik AYOUBI ◽  
M. P. Sandra MEULEMANS ◽  
Wim J. M. VAN DE VEN
Keyword(s):  
Transcription Factor ◽  
Promoter Region ◽  
Promoter Activity ◽  
Secretory Pathway ◽  
Tata Box ◽  
Proximal Promoter ◽  
Prohormone Convertase ◽  
Specific Expression ◽  
Proximal Promoter Region ◽  
Prohormone Convertase 2

Prohormone convertases are involved in the tissue-specific endoproteolytic processing of prohormones and neuropeptide precursors within the secretory pathway. In the present study, we have isolated genomic clones comprising the 5ʹ-terminal region of the human prohormone convertase 2 (PC2) gene and established characteristics of the PC2 promoter region. The proximal promoter region is very G+C-rich and does not contain a canonical TATA box or a CAAT box. Transient expression assays with a set of human PC2 gene fragments containing progressive 5ʹ deletions demonstrate that the proximal promoter region is capable of directing high levels of neuroendocrine-specific expression of reporter gene constructs. In addition, we show that the transcription factor EGR-1 interacts with two distinct elements within the proximal human PC2 promoter region. Transfection experiments also demonstrate that EGR-1 is able to enhance PC2 promoter activity.

scholarly journals The ER-associated protease Ste24 prevents N-terminal signal peptide-independent translocation into the endoplasmic reticulum in Saccharomyces cerevisiae

2020 ◽  
Vol 295 (30) ◽  
pp. 10406-10419 ◽  
Author(s):  
Akira Hosomi ◽  
Kazuko Iida ◽  
Toshihiko Cho ◽  
Hidetoshi Iida ◽  
Masashi Kaneko ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Endoplasmic Reticulum ◽  
Transcription Factor ◽  
Signal Peptide ◽  
Secretory Pathway ◽  
Soluble Proteins ◽  
Signal Peptides ◽  
Yeast Mutant ◽  
The Past ◽  
Reporter Proteins

Soluble proteins destined for the secretory pathway contain an N-terminal signal peptide that induces their translocation into the endoplasmic reticulum (ER). The importance of N-terminal signal peptides for ER translocation has been extensively examined over the past few decades. However, in the budding yeast Saccharomyces cerevisiae, a few proteins devoid of a signal peptide are still translocated into the ER and then N-glycosyl-ated. Using signal peptide-truncated reporter proteins, here we report the detection of significant translocation of N-terminal signal peptide-truncated proteins in a yeast mutant strain (ste24Δ) that lacks the endopeptidase Ste24 at the ER membrane. Furthermore, several ER/cytosolic proteins, including Sec61, Sec66, and Sec72, were identified as being involved in the translocation process. On the basis of screening for 20 soluble proteins that may be N-glycosylated in the ER in the ste24Δ strain, we identified the transcription factor Rme1 as a protein that is partially N-glycosylated despite the lack of a signal peptide. These results clearly indicate that some proteins lacking a signal peptide can be translocated into the ER and that Ste24 typically suppresses this process.

scholarly journals The liverwort oil body is formed by redirection of the secretory pathway

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Takehiko Kanazawa ◽  
Hatsune Morinaka ◽  
Kazuo Ebine ◽  
Takashi L. Shimada ◽  
Sakiko Ishida ◽  
...  
Keyword(s):  
Phase Transition ◽  
Transcription Factor ◽  
Secretory Pathway ◽  
Physiological Function ◽  
Eukaryotic Cells ◽  
Marchantia Polymorpha ◽  
Oil Body ◽  
Body Formation ◽  
Common Strategy

AbstractEukaryotic cells acquired novel organelles during evolution through mechanisms that remain largely obscure. The existence of the unique oil body compartment is a synapomorphy of liverworts that represents lineage-specific acquisition of this organelle during evolution, although its origin, biogenesis, and physiological function are yet unknown. We find that two paralogous syntaxin-1 homologs in the liverwort Marchantia polymorpha are distinctly targeted to forming cell plates and the oil body, suggesting that these structures share some developmental similarity. Oil body formation is regulated by an ERF/AP2-type transcription factor and loss of the oil body increases M. polymorpha herbivory. These findings highlight a common strategy for the acquisition of organelles with distinct functions in plants, via periodical redirection of the secretory pathway depending on cellular phase transition.

scholarly journals Switching secretory pathway direction for organelle acquisition in plants

2020 ◽  
Author(s):  
Takehiko Kanazawa ◽  
Hatsune Morinaka ◽  
Kazuo Ebine ◽  
Takashi L. Shimada ◽  
Sakiko Ishida ◽  
...  
Keyword(s):  
Phase Transition ◽  
Transcription Factor ◽  
Secretory Pathway ◽  
Physiological Function ◽  
Eukaryotic Cells ◽  
Marchantia Polymorpha ◽  
Oil Body ◽  
Body Formation ◽  
Common Strategy

AbstractEukaryotic cells acquired novel organelles during evolution through mechanisms that remain largely obscure. The existence of the unique oil body compartment is a synapomorphy of liverworts that represents lineage-specific acquisition of this organelle during evolution, although its origin, biogenesis, and physiological function are yet unknown. We found that two Syntaxin 1 paralogs in the liverwort, Marchantia polymorpha, are distinctly targeted to forming cell plates and the oil body, suggesting these structures share some developmental similarity. Oil body formation is under the regulation of an ERF/AP2-type transcription factor and loss of the oil body increased M. polymorpha herbivory. These findings highlight a common strategy for the acquisition of organelles with distinct functions in plants, via periodical switching in secretion direction depending on cellular phase transition.

scholarly journals GSK-3–mediated phosphorylation couples ER–Golgi transport and nuclear stabilization of the CREB-H transcription factor to mediate apolipoprotein secretion

2017 ◽  
Vol 28 (11) ◽  
pp. 1565-1579 ◽  
Author(s):  
Sónia Barbosa ◽  
Suzanne Carreira ◽  
Peter O’Hare
Keyword(s):  
Transcription Factor ◽  
Nuclear Import ◽  
Metabolic Pathways ◽  
Secretory Pathway ◽  
Integrated Control ◽  
Active Form ◽  
Transcriptional Responses ◽  
Golgi Transport ◽  
Er Retention ◽  
Drug Inhibition

CREB-H, an ER-anchored transcription factor, plays a key role in regulating secretion in metabolic pathways, particularly triglyceride homeostasis. It controls the production both of secretory pathway components and cargoes, including apolipoproteins ApoA-IV and ApoC-II, contributing to VLDL/HDL distribution and lipolysis. The key mechanism controlling CREB-H activity involves its ER retention and forward transport to the Golgi, where it is cleaved by Golgi-resident proteases, releasing the N-terminal product, which traffics to the nucleus to effect transcriptional responses. Here we show that a serine-rich motif termed the P-motif, located in the N-terminus between serines 73 and 90, controls release of the precursor transmembrane form from the ER and its forward transport to the Golgi. This motif is subject to GSK-3 phosphorylation, promoting ER retention, while mutation of target serines and drug inhibition of GSK-3 activity coordinately induce both forward transport of the precursor and cleavage, resulting in nuclear import. We previously showed that for the nuclear product, the P-motif is subject to multiple phosphorylations, which regulate stability by targeting the protein to the SCFFbw1a E3 ubiquitin ligase. Thus phosphorylation at the P-motif provides integrated control of CREB-H function, coupling intercompartmental transport in the cytoplasm with stabilization of the active form in the nucleus.

Transcription factor/DNA interactions visualized by electron spectroscopic imaging

1992 ◽  
Vol 50 (1) ◽  
pp. 450-451
Author(s):  
David P. Bazett-Jones ◽  
Mark L. Brown
Keyword(s):  
Transcription Factor ◽  
Dna Sequences ◽  
Transcription Initiation ◽  
Molecular Mechanisms ◽  
Phosphorus Content ◽  
Spectroscopic Imaging ◽  
Electron Spectroscopic Imaging ◽  
Dna Backbone ◽  
Two Parameters ◽  
High Level

A multisubunit RNA polymerase enzyme is ultimately responsible for transcription initiation and elongation of RNA, but recognition of the proper start site by the enzyme is regulated by general, temporal and gene-specific trans-factors interacting at promoter and enhancer DNA sequences. To understand the molecular mechanisms which precisely regulate the transcription initiation event, it is crucial to elucidate the structure of the transcription factor/DNA complexes involved. Electron spectroscopic imaging (ESI) provides the opportunity to visualize individual DNA molecules. Enhancement of DNA contrast with ESI is accomplished by imaging with electrons that have interacted with inner shell electrons of phosphorus in the DNA backbone. Phosphorus detection at this intermediately high level of resolution (≈lnm) permits selective imaging of the DNA, to determine whether the protein factors compact, bend or wrap the DNA. Simultaneously, mass analysis and phosphorus content can be measured quantitatively, using adjacent DNA or tobacco mosaic virus (TMV) as mass and phosphorus standards. These two parameters provide stoichiometric information relating the ratios of protein:DNA content.

The role of transcription factor Egr‐1 in IL‐1 up‐regulation of tubular CD44 expression

Nephrology ◽  
2000 ◽  
Vol 5 (3) ◽  
pp. A92-A92
Author(s):  
Takazoe K ◽  
Foti R ◽  
Hurst La ◽  
Atkins Rc ◽  
Nikolic‐Paterson DJ.
Keyword(s):  
Transcription Factor ◽  
Cd44 Expression
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