Luman is capable of binding and activating transcription from the unfolded protein response element

DenBoer, Lisa M.; Hardy-Smith, Philip W.; Hogan, Melissa R.; Cockram, Gregory P.; Audas, Timothy E.; Lu, Rui

doi:10.1016/j.bbrc.2005.03.141

Cited by 85 publications

(74 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Results from EMSA show that LZIP binds to the C/EBP element in CCR2 pro-moter, indicating that LZIP functions as a transcription factor that binds to the C/EBP element of CCR2 and accelerates the transcriptional activation of CCR2. Although further studies are required to characterize the exact regulatory mechanism of LZIP in expression of chemokine receptors, our data are consistent with previous results that LZIP binds C/EBP element (DenBoer et al, 2005).…”

Section: Discussionsupporting

confidence: 91%

See 1 more Smart Citation

Human LZIP induces monocyte CC chemokine receptor 2 expression leading to enhancement of monocyte chemoattractant protein 1/CCL2-induced cell migration

et al. 2008

View full text Add to dashboard Cite

Chemokines and chemokine receptors play a role in migration of circulating leukocytes to the region of inflammation. Human LZIP is an uncharacterized transcription factor and is known to participate in leukotactin (Lkn)-1/CCL15-induced cell migration. We investigated the role of human LZIP in expression of CC chemokine receptors (CCRs) and its involvement in monocyte migration. RNase protection analysis showed that LZIP increased mRNA expression of CCR2 and CCR1 in THP-1 cells. Surface expressions of both CCR2 and CCR1 were also increased by LZIP. Results from an electrophoretic mobility shift assay showed that LZIP binds to the C/EBP element in the CCR2 promoter. LZIP also enhanced the chemotactic activities of monocyte chemoattractant protein-1/CCL2 and Lkn-1. These results suggest that LZIP regulates expression of chemokine receptors that are involved in monocyte migration.

show abstract

Section: Discussionsupporting

confidence: 91%

“…LZIP is a basic leucine zipper transcription factor that binds consensus DNA elements, such as CRE, AP-1 and C/EBP (DenBoer et al, 2005). Based on reports regarding the nucleotide sequence of the human CCR2 gene (Yamato et al, 1999), C/EBP elements exist in CCR2 promoter.…”

Section: Discussionmentioning

confidence: 99%

Human LZIP induces monocyte CC chemokine receptor 2 expression leading to enhancement of monocyte chemoattractant protein 1/CCL2-induced cell migration

et al. 2008

View full text Add to dashboard Cite

show abstract

“…91 In higher eukaryotes, the UPR expanded to a signal transduction nexus: IRE1 and ATF6 both contain a and b isoforms. Several b-ZIP transcription factors that share homology with ATF6, such as Luman, 102 are reported to be ER stress responsive. To cope with different types of ER stress in different tissues, vertebrates have also evolved tissue-specific UPR regulators.…”

Section: Discussionmentioning

confidence: 99%

From acute ER stress to physiological roles of the Unfolded Protein Response

2006

View full text Add to dashboard Cite

When protein folding in the endoplasmic reticulum (ER) is disrupted by alterations in homeostasis in the ER lumen, eucaryotic cells activate a series of signal transduction cascades that are collectively termed the unfolded protein response (UPR). Here we summarize our current understanding of how the UPR functions upon acute and severe stress. We discuss the mechanism of UPR receptor activation, UPR signal transduction to translational and transcriptional responses, UPR termination, and UPR signals that activate upon irreversible damage. Further, we review recent studies that have revealed that UPR provides a wide spectrum of physiological roles. Each individual UPR subpathway provides a unique and specialized role in diverse developmental and metabolic processes. This is especially observed for professional secretory cells, such as plasma cells, pancreatic b cells, hepatocytes, and osteoblasts, where high-level secretory protein synthesis requires a highly evolved mechanism to properly fold, process, and secrete proteins. There is a growing body of data that suggest that different subpathways of the UPR are required throughout the entire life of eucaryotic organisms, from regulation of differentiation to induction of apoptosis.

show abstract

“…A candidate is CREB3 (or Luman), which can bind to the UPR responsive element, but is not activated by classical UPR stimulants such as tunicamycin or thapsigargin (DenBoer et al, 2005). But are there others?…”

Section: Discussionmentioning

confidence: 99%

Regulated increase in folding capacity prevents unfolded protein stress in the ER

Christis

Fullaondo

Schildknegt

et al. 2010

Journal of Cell Science

View full text Add to dashboard Cite

SummaryStimulation of thyrocytes with thyroid stimulating hormone (TSH) leads to a morphological change and a massive increase in thyroglobulin (Tg) production. Although Tg is a demanding client of the endoplasmic reticulum (ER), its increase did not result in significant accumulation of unfolded protein in the ER. Instead, ER chaperones and folding enzymes reached maximum synthesis rates immediately after TSH stimulation, before significant upregulation of Tg synthesis. The resulting increase in folding capacity before client protein production prevented cellular unfolded-protein stress, confirmed by the silence of the most conserved branch of the unfolded protein response. Thyrocytes set an example of physiological adaptation of cells to a future potentially stress-causing situation, which suggests a general strategy for both non-secretory and specialized secretory cells.

show abstract

Luman is capable of binding and activating transcription from the unfolded protein response element

Cited by 85 publications

References 31 publications

Human LZIP induces monocyte CC chemokine receptor 2 expression leading to enhancement of monocyte chemoattractant protein 1/CCL2-induced cell migration

Human LZIP induces monocyte CC chemokine receptor 2 expression leading to enhancement of monocyte chemoattractant protein 1/CCL2-induced cell migration

From acute ER stress to physiological roles of the Unfolded Protein Response

Regulated increase in folding capacity prevents unfolded protein stress in the ER

Contact Info

Product

Resources

About