Crm1p mediates regulated nuclear export of a yeast AP-1-like transcription factor

Yan, Catherine T.; Lee, Linda H.; Davis, Laura I.

doi:10.1093/emboj/17.24.7416

Cited by 234 publications

(277 citation statements)

References 96 publications

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“…Yap1p [9], the prototypical YAP gene family, which regulates the yeast oxidative stress response regulon, also regulates the expression of YCF1. Yap1p primary control lies in a redox-regulated Crm1-dependent nuclear export [10][11][12]. Redox signals disrupt the Yap1p-chromosome region maintenance protein (Crm1p) interaction through a redoxdependent alteration of the Yap1p C-terminal nuclear export signal (NES), thereby promoting Yap1 nuclear accumulation.…”

Section: Introductionmentioning

confidence: 99%

Yap8p activation in Saccharomyces cerevisiae under arsenic conditions

MENEZES¹

2004

FEBS Letters

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Yap8p, a member of the Saccharomyces cerevisiae Yap family, is activated in response to arsenic. Both the mechanisms by which this activation takes place and its regulation have not yet been identified. In this report, we show that Yap8p is not activated at the transcriptional level but, rather, its nuclear transport is actively regulated and dependent on the exportin chromosome region maintenance protein. In addition, it is shown that Cys 132 , Cys 137 and Cys 274 are essential for Yap8p localization and transactivation function both of which are required for its biological activity.

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Section: Introductionmentioning

confidence: 99%

Yap8p activation in Saccharomyces cerevisiae under arsenic conditions

MENEZES¹

2004

FEBS Letters

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“…Three previously known Xpo1 interaction partners (Yap1, Nup42, and Nup49) were identified, demonstrating the usefulness of the two-hybrid method for this purpose. Yap1 contains a nuclear export sequence of the leucine-rich type and acts as an export substrate for Xpo1 (76) whereas Nup42 and Nup49 (48) are structural components of the nuclear pore complex (NPC) through which all nucleocytoplasmic trafficking occurs (18,69). Sgm1, Sla2, Spc72, Ltv1, and Hpa3 represent novel interaction partners for Xpo1.…”

Section: Resultsmentioning

confidence: 99%

“…In contrast, few NES-containing proteins have been identified in Saccharomyces cerevisiae. Although the budding yeast Crm1 orthologue Xpo1 is involved in nuclear export of Hog1 (19), Yap1 (76), Ssb1 (62), Ace2 (36), and Prp40 (46), few of the NESs involved have been characterized at a molecular level.…”

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confidence: 99%

Nuclear Export Receptor Xpo1/Crm1 Is Physically and Functionally Linked to the Spindle Pole Body in Budding Yeast

Neuber

Franke

Wittstruck

et al. 2008

Molecular and Cellular Biology

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The spindle pole body (SPB) represents the microtubule organizing center in the budding yeast Saccharomyces cerevisiae. It is a highly structured organelle embedded in the nuclear membrane, which is required to anchor microtubules on both sides of the nuclear envelope. The protein Spc72, a component of the SPB, is located at the cytoplasmic face of this organelle and serves as a receptor for the ␥-tubulin complex. In this paper we show that it is also a binding partner of the nuclear export receptor Xpo1/Crm1. Xpo1 binds its cargoes in a Ran-dependent fashion via a short leucine-rich nuclear export signal (NES). We show that binding of Spc72 to Xpo1 depends on Ran-GTP and a functional NES in Spc72. Mutations in this NES have severe consequences for mitotic spindle morphology in vivo. This is also the case for xpo1 mutants, which show a reduction in cytoplasmic microtubules. In addition, we find a subpopulation of Xpo1 localized at the SPB. Based on these data, we propose a functional link between Xpo1 and the SPB and discuss a role for this exportin in spindle biogenesis in budding yeast.In eukaryotes, the movement of proteins and RNAs between the nucleus and the cytoplasm is an essential cellular process that is mediated by soluble transport receptors (26,52). In addition, the small GTPase Ran (Gsp1 in yeast) and its cytoplasmic and nuclear effectors are needed (12). Transport receptors involved in nuclear import reactions are usually termed importins, and they recognize their cargoes via a specific amino acid motif, the nuclear localization sequence, or NLS. By analogy, nuclear export reactions are mediated by so-called exportins. Xpo1 (also known as Crm1) was one of the first nuclear export receptors to be identified (23,27,50,64) and recognizes a short leucine-rich amino acid sequence on its cargo, called a nuclear export signal, or NES. Numerous export cargoes have now been identified for the mammalian Crm1 protein, including protein kinase A inhibitor PKI, p53, and the human immunodeficiency virus protein Rev (20,25,66). In addition, Crm1 is involved in the nuclear export of several classes of RNAs such as viral pre-mRNAs, ribosomal RNAs, and snRNAs (54). In contrast, few NES-containing proteins have been identified in Saccharomyces cerevisiae. Although the budding yeast Crm1 orthologue Xpo1 is involved in nuclear export of Hog1 (19), Yap1 (76), Ssb1 (62), Ace2 (36), and Prp40 (46), few of the NESs involved have been characterized at a molecular level.Recently, alongside its well-established role in nuclear export, mammalian Crm1 was shown to be involved in the control of centrosome duplication (71). Centrosomes function as microtubule (MT) organizing centers in mammalian somatic cells and direct the formation of a bipolar spindle during mitosis (reviewed in reference 6). In another study, Crm1 was found to bind to kinetochores, complex protein assemblies that are needed to establish the attachment of MTs to chromatin (4). These studies point to an unanticipated role of the exportin Crm1 in control of spin...

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“…[lexA ] [25] and one of the following pJG4-5 [B42AD haemagglutinin (HA) epitope tag TRP1] [5] or YAP2-B42. To create the YAP2-B42 chimera, XhoI restriction sites were introduced by PCR and the product was cloned into the vector pJG4-5 [24].…”

Section: Two-hybrid Assaymentioning

confidence: 99%

“…3C) and reintroducing YAP2 into Dyap2Dfrm2 [5]; the cysteine residues present in both cCRDs are in bold, note that Yap2 has an additional cysteine (Cys391 -in bold and underlined). (B) Sensitivity assays of Dyap1Dyap2 strain transformed with the fusions GFP-Yap1 or GFP-Yap1-cCRDYap2 (diagrammed in Fig.…”

Section: Yap2 Ccrd Cys 356 Cysmentioning

confidence: 99%

The S. cerevisiae Yap1 and Yap2 transcription factors share a common cadmium‐sensing domain

et al. 2006

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Towards elucidating the function of Yap2, which remains unclear, we have taken advantage of the C-terminal homology between Yap1 and Yap2. Swapping domains experiments show that the Yap2 C-terminal domain functionally substitutes for the homologous Yap1 domain in the response to Cd, but not to H 2 O 2 . We conclude that specificity determinants of the Cd response are encoded within both Yap1 and Yap2 Cterminus, whereas those required for H 2 O 2 response are only present in the Yap1 C-terminus. Furthermore, our results identify FRM2 as Cd-responsive Yap2 target and indicate a possible role of this protein in regulating a metal stress response.

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Crm1p mediates regulated nuclear export of a yeast AP-1-like transcription factor

Cited by 234 publications

References 96 publications

Yap8p activation in Saccharomyces cerevisiae under arsenic conditions

Yap8p activation in Saccharomyces cerevisiae under arsenic conditions

Nuclear Export Receptor Xpo1/Crm1 Is Physically and Functionally Linked to the Spindle Pole Body in Budding Yeast

The S. cerevisiae Yap1 and Yap2 transcription factors share a common cadmium‐sensing domain

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