A Novel Creb Family Gene Telomeric of HLA-DRA in the HLA Complex

Min, Jingjuan; Shukla, Hridayabhiranjan; Kozono, Haruo; Bronson, Sarah K.; Weissman, Sherman M.; Chaplin, David

doi:10.1006/geno.1995.9891

Cited by 32 publications

(25 citation statements)

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“…The percentages of identity for domains are shown between the genes compared. Besides these regions, a serine-rich section of CREB-RP was noted (56% serine) (20). As shown, there is also a serine-rich region in ATF6 (41% serine), but there is no significant direct amino acid sequence similarity in this region.…”

Section: Screen For Srf-interacting Proteins In Yeastmentioning

confidence: 88%

“…5B), it contains no similarity to those genes outside of this region. The CREB-RP (G13) gene was identified during extensive cloning and sequencing of the human HLA locus (17,20). Its expression was detected in all the cell lines and tissues tested (20).…”

Section: Discussionmentioning

confidence: 99%

“…This basic-leucine zipper region is similar to those of more than 30 members of the leucine zipper superfamily currently in the GenBank database. The sequence is most similar to that of CREB-RP (also called G13), a CREB-related gene cloned in the HLA locus (17,20). Otherwise, the highest similarities are to ATF-1, CREB, and CREM (4,19,29) (Fig.…”

Section: Screen For Srf-interacting Proteins In Yeastmentioning

confidence: 99%

“…A sequence alignment of the mammalian proteins most similar to ATF6 in the basic-leucine zipper domain in a BLAST search of the GenBank database is shown. ATF6 is most similar to CREB-RP (also called G13) (17,20), followed by human ATF-1 (29), human CREB (19), and human CREM (4). In this region, ATF6 has 61% identity and 84% similarity to human CREB-RP, 44% identity and 69% similarity to ATF-1, 42% identity and 72% similarity to CREM, and 40% identity and 65% similarity to CREB.…”

Section: Screen For Srf-interacting Proteins In Yeastmentioning

confidence: 99%

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Interaction of ATF6 and serum response factor

Zhu

Johansen

Prywes

1997

Molecular and Cellular Biology

151

136

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Serum response factor (SRF) is a transcription factor which binds to the serum response element (SRE) in the c-fos promoter. It is required for regulated expression of the c-fos gene as well as other immediate-early genes and some tissue-specific genes. To better understand the regulation of SRF, we used a yeast interaction assay to screen a human HeLa cell cDNA library for SRF-interacting proteins. ATF6, a basic-leucine zipper protein, was isolated by binding to SRF and in particular to its transcriptional activation domain. The binding of ATF6 to SRF was also detected in vitro. An ATF6-VP16 chimera activated expression of an SRE reporter gene in HeLa cells, suggesting that ATF6 can interact with endogenous SRF. More strikingly, an antisense ATF6 construct reduced serum induction of a c-fos reporter gene, suggesting that ATF6 is involved in activation of transcription by SRF. ATF6 was previously partially cloned as a member of the ATF family. The complete cDNA of ATF6 was isolated, and its expression pattern was described.Expression of the c-fos gene is rapidly transcriptionally activated in serum-starved cells by serum and many other mitogens. Mapping of the c-fos promoter suggests that a key sequence element is the serum response element (SRE) (15). SRE-like elements have also been found to be critical for the expression of other immediate-early genes, a number of muscle-specific genes, and interleukin-2 receptor (15). The main nuclear protein found to bind the SRE is serum response factor (SRF). SRF is a 508-amino-acid protein of the MADS box family that binds to DNA as a dimer (21). In addition to central DNA binding and dimerization domains (spanning the conserved MADS box), it contains a C-terminal transcriptional activation domain (13).One mechanism for serum induction of the SRE is through a family of SRF-associated proteins, ternary complex factors (TCFs) (27). TCFs are encoded by three related genes (Elk1, Sap1, and Sap2/Net/Erp) with ets-related DNA binding domains (22,27). TCFs contact both SRF and a specific sequence element and bind to SRF only when a DNA binding site is adjacent to the SRF site. TCFs also contain a transcriptional activation domain which is regulated by protein kinases from the mitogen-activated protein kinase family (27,28). Activation of c-fos expression by serum and various growth factors at least partially works by activating mitogen-activated protein kinases. A mutation of the TCF site in the c-fos promoter, however, does not have a large effect on serum induction of a reporter gene (6,11). This and other results suggest that there is a TCF-independent mechanism for serum induction of c-fos (10,12,14).The TCF transcriptional activation domain acts in conjunction with the transcriptional activation domain of SRF to increase c-fos transcription (9,12,14). The transcriptional activation domain of SRF can also function alone when it is fused to the DNA binding domain of GAL4, but it is not regulated by serum in this context (13). One mechanism for the activation of transcription...

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Section: Screen For Srf-interacting Proteins In Yeastmentioning

confidence: 88%

Section: Discussionmentioning

confidence: 99%

Section: Screen For Srf-interacting Proteins In Yeastmentioning

confidence: 99%

Section: Screen For Srf-interacting Proteins In Yeastmentioning

confidence: 99%

See 2 more Smart Citations

Interaction of ATF6 and serum response factor

Zhu

Johansen

Prywes

1997

Molecular and Cellular Biology

151

136

View full text Add to dashboard Cite

show abstract

“…It was previously reported (28) that mammalian cells express another bZIP protein closely related to ATF6, which is encoded by the cyclic AMP response element binding proteinrelated protein (CREB-RP) gene (17) (also called the G13 gene [9]). Our recent study revealed that this gene product also functions as an inducible component of ERSF, and we thus proposed calling the ATF6 gene product ATF6␣ and the CREB-RP (G13) gene product ATF6␤ (K. Haze, T. Okada, H. Yoshida, H. Yanagi, T. Yura, M. Negishi, and K. Mori, submitted for publication).…”

mentioning

confidence: 99%

Endoplasmic Reticulum Stress-Induced Formation of Transcription Factor Complex ERSF Including NF-Y (CBF) and Activating Transcription Factors 6α and 6β That Activates the Mammalian Unfolded Protein Response

Yoshida

Okada

Haze

et al. 2001

Molecular and Cellular Biology

278

191

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The levels of molecular chaperones and folding enzymes in the endoplasmic reticulum (ER) are controlled by a transcriptional induction process termed the unfolded protein response (UPR). The mammalian UPR is mediated by the cis-acting ER stress response element (ERSE), the consensus sequence of which is CCAAT-N 9 -CCACG. We recently proposed that ER stress response factor (ERSF) binding to ERSE is a heterologous protein complex consisting of the constitutive component NF-Y (CBF) binding to CCAAT and an inducible component binding to CCACG and identified the basic leucine zipper-type transcription factors ATF6␣ and ATF6␤ as inducible components of ERSF. ATF6␣ and ATF6␤ produced by ER stress-induced proteolysis bind to CCACG only when CCAAT is bound to NF-Y, a heterotrimer consisting of NF-YA, NF-YB, and NF-YC. Interestingly, the NF-Y and ATF6 binding sites must be separated by a spacer of 9 bp. We describe here the basis for this strict requirement by demonstrating that both ATF6␣ and ATF6␤ physically interact with NF-Y trimer via direct binding to the NF-YC subunit. ATF6␣ and ATF6␤ bind to the ERSE as a homo-or heterodimer. Furthermore, we showed that ERSF including NF-Y and ATF6␣ and/or ␤ and capable of binding to ERSE is indeed formed when the cellular UPR is activated. We concluded that ATF6 homo-or heterodimers recognize and bind directly to both the DNA and adjacent protein NF-Y and that this complex formation process is essential for transcriptional induction of ER chaperones.Two mammalian proteins with molecular masses of 78 and 94 kDa identified in the mid-1970s were named glucose-regulated proteins (GRP78 and GRP94, respectively) due to the marked increases in their levels on depletion of glucose from media for cell culture (24). Subsequent studies indicated that this phenomenon is part of the cellular response to the accumulation of unfolded proteins in the endoplasmic reticulum (ER) (8, 18). Not only glucose deprivation but also various physiological and environmental stress conditions (ER stress) cause unfolding or misfolding of proteins in the ER, where newly synthesized secretory and transmembrane proteins fold and assemble. As only correctly folded molecules are allowed to move along the secretory pathway, eukaryotic cells must deal with protein misfolding in the ER promptly and appropriately to avoid malfunction and/or mislocalization of proteins that are synthesized on membrane-bound ribosomes and translocated into the ER. A typical cellular strategy to cope with unfolded proteins in the ER is induction of molecular chaperones and folding enzymes localized in the lumen of the ER, such as BiP/GRP78 and GRP94, resulting in augmentation of the folding capacity of the ER. This homeostatic response is achieved by a transcriptional induction process coupled with signaling from the ER to the nucleus, now known as the unfolded protein response (UPR).The transcriptional apparatus responsible for the mammalian UPR was poorly understood until the cis-acting ER stress response element (ERSE), necessary and ...

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A review of the mammalian unfolded protein response

Chakrabarti

Chen

Varner

2011

Biotech & Bioengineering

362

331

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Proteins requiring post-translational modifications such as N-linked glycosylation are processed in the endoplasmic reticulum (ER). A diverse array of cellular stresses can lead to dysfunction of the ER and ultimately to an imbalance between protein-folding capacity and protein-folding load. Cells monitor protein folding by an inbuilt quality control system involving both the ER and the Golgi apparatus. Unfolded or misfolded proteins are tagged for degradation via ER associated degradation (ERAD) or sent back through the folding cycle. Continued accumulation of incorrectly folded proteins can also trigger the Unfolded Protein Response (UPR). In mammalian cells, UPR is a complex signaling program mediated by three ER transmembrane receptors: activating transcription factor 6 (ATF6), inositol requiring kinase 1 (IRE1) and double-stranded RNA-activated protein kinase (PKR)-like endoplasmic reticulum kinase (PERK). UPR performs three functions, adaptation, alarm and apoptosis. During adaptation, the UPR tries to reestablish folding homeostasis by inducing the expression of chaperones that enhance protein folding. Simultaneously, global translation is attenuated to reduce the ER folding load while the degradation rate of unfolded proteins is increased. If these steps fail, the UPR induces a cellular alarm and mitochondrial mediated apoptosis program. UPR malfunctions have been associated with a wide range of disease states including tumor progression, diabetes, as well as immune and inflammatory disorders. This review describes recent advances in understanding the molecular structure of UPR in mammalian cells, its functional role in cellular stress, and its pathophysiology.

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A Novel Creb Family Gene Telomeric of HLA-DRA in the HLA Complex

Cited by 32 publications

References 0 publications

Interaction of ATF6 and serum response factor

Interaction of ATF6 and serum response factor

Endoplasmic Reticulum Stress-Induced Formation of Transcription Factor Complex ERSF Including NF-Y (CBF) and Activating Transcription Factors 6α and 6β That Activates the Mammalian Unfolded Protein Response

A review of the mammalian unfolded protein response

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