Human GTSE-1 Regulates p21CIP1/WAF1 Stability Conferring Resistance to Paclitaxel Treatment

Bublik, Debora Rosa; Scolz, M; Triolo, Gianluca; Monte, Martín; Schneider, Claudio

doi:10.1074/jbc.m109.045948

Cited by 39 publications

(38 citation statements)

References 31 publications

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“…In addition to radiation resistance, FKBPL plays a significant role in tumor progression (Robson et al 1997;Robson et al 1999;Robson et al 2000;Jascur et al 2005). In tumor cells, FKBPL appears to participate in not only growth of the tumor, but also in the sensitivity of the tumor to various chemotherapeutic agents (Bublik et al 2010). For example, high levels of GSTE-1 interact with the FKBPL/ Hsp90/p21 complex, which leads to p21 stabilization leading to resistance to the chemotherapeutic agent Taxane (Bublik et al 2010).…”

Section: Fkbplmentioning

confidence: 98%

“…In tumor cells, FKBPL appears to participate in not only growth of the tumor, but also in the sensitivity of the tumor to various chemotherapeutic agents (Bublik et al 2010). For example, high levels of GSTE-1 interact with the FKBPL/ Hsp90/p21 complex, which leads to p21 stabilization leading to resistance to the chemotherapeutic agent Taxane (Bublik et al 2010). Although the exact radio-and chemo-protective role of FKBPL needs to be elucidated, the data clearly show that FKBPL is an important factor in cell-cycle progression, cell survival, and tumor progression.…”

Section: Fkbplmentioning

confidence: 99%

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Functions of the Hsp90-Binding FKBP Immunophilins

Guy

Garcia

Sivils

et al. 2014

Subcellular Biochemistry

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Hsp90 functionally interacts with a broad array of client proteins, but in every case examined Hsp90 is accompanied by one or more co-chaperones. One class of co-chaperone contains a tetratricopeptide repeat domain that targets the co-chaperone to the C-terminal region of Hsp90. Within this class are Hsp90-binding peptidylprolyl isomerases, most of which belong to the FK506-binding protein (FKBP) family. Despite the common association of FKBP co-chaperones with Hsp90, it is now clear that the client protein influences, and is influenced by, the particular FKBP bound to Hsp90. Examples include Xap2 in aryl hydrocarbon receptor complexes and FKBP52 in steroid receptor complexes. In this chapter, we discuss the known functional roles played by FKBP co-chaperones and, where possible, relate distinctive functions to structural differences between FKBP members.

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Section: Fkbplmentioning

confidence: 98%

Section: Fkbplmentioning

confidence: 99%

Functions of the Hsp90-Binding FKBP Immunophilins

Guy

Garcia

Sivils

et al. 2014

Subcellular Biochemistry

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“…, and a reduction in the DNA repair 191,192 . All of these FKBPL-related roles are associated with intracellular FKBPL however more recently, an extracellular role for FKBPL was identified.…”

Section: The Role Of Ppiases In Cancermentioning

confidence: 99%

The Role of Peptidyl Prolyl Isomerases in Aging and Vascular Diseases

McClements¹,

Annett²,

Yakkundi³

et al. 2015

CMP

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Peptidyl prolyl isomerases (PPIases) are proteins belonging to the immunophilin family and are characterised by their cis-trans isomerization activity at the X-Pro peptide bond, in addition to their tetratricopeptide repeat (TPR) domain, important for interaction with the molecular chaperone, Hsp90. Due to this unique structure these proteins are able to facilitate proteinprotein interactions which can impact significantly on a range of cellular processes such as cell signalling, differentiation, cell cycle progression, metabolic activity and apoptosis.Malfunction and/or dysregulation of most members of this class of proteins promotes cellular damage and tissue/organ failure, predisposing to ageing and age-related diseases. Many individual genes within the PPIase family are associated with several age-related diseases including cardiovascular diseases (CVDs), atherosclerosis, type II diabetes (T2D), chronic kidney disease (CDK), neurodegeneration, cancer and age-related macular degeneration (AMD), in addition to the ageing process itself. This review will focus on the different roles of PPIases, and their therapeutic/biomarker potential in these age-related vascular diseases.

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“…A number of publications have demonstrated that this transport mechanism first proposed for the GR is used by several other factors such as the AAV-2 (adeno-associated virus-2) [66], poly-glutamine aggregated proteins in Kennedy disease cells [67], the brain specific protein PAHX-AP1 [68], the proapoptotic factor p53 [65], the cell cycle arresting protein p21 [69], the mineralocorticoid receptor (MR) [36], FKBPL/DIR1/WisP39 client proteins [62], the transcription factor RAC3 [70], the ecdysone receptor [71], and so on. Moreover, the interaction between dynein and IMMs has also been found in plants [72], suggesting that the functional role of this complex has been preserved during the evolution.…”

Section: The Hsp90•fkbp52•dynein/dynactin Molecular Machinery Of Tranmentioning

confidence: 99%

“…In addition to radiation resistance, FKBPL/WisP39 plays a significant role in tumor progression [150,152,155,157]. In tumor cells, FKBPL/WisP39 favors the tumor growth and it is also related to the sensitivity of the tumor to chemotherapeutic compounds [158].…”

Section: Tpr-domain Immunophilins In Cancermentioning

confidence: 99%

The Emerging Role of TPR-Domain Immunophilins in the Mechanism of Action of Steroid Receptors

Mazaira

Lagadari

Erlejman

et al. 2014

Nuclear Receptor Research

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Abstract. In the absence of ligand, some members of nuclear receptor family such as corticosteroid receptors are primarily located in the cytoplasm, and they rapidly accumulate in the nucleus upon ligand-binding. Other members of the family such as the estrogen receptor are mostly nuclear. Regardless of their primary location, these oligomeric proteins undergo a dynamic nuclearcytoplasmic shuttling, and their transport through the cytoplasmic compartment has always been assumed to occur in a stochastic manner by simple diffusion. Although heuristic, this oversimplified model has never been demonstrated. Moreover, it has always been assumed that the first step related to receptor activation is the dissociation of the Hsp90-based heterocomplex, a process referred to as 'transformation.' Nonetheless, recent experimental evidence indicates that the chaperone machinery is required for the retrotransport of the receptor throughout the cytoplasm and facilitates its active passage through the nuclear pore. Therefore, transformation is actually a nuclear event. A group of Hsp90-binding cochaperones belonging to the immunophilin family plays a cardinal role not only in the mechanism for receptor movement, but also in nuclear events leading to interactions with nuclear sites of action and the regulation of transcriptional activity. In this article we analyze the importance of molecular chaperones and TPR-domain immunophilins in the molecular mechanism of action of steroid receptors.

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Human GTSE-1 Regulates p21CIP1/WAF1 Stability Conferring Resistance to Paclitaxel Treatment

Cited by 39 publications

References 31 publications

Functions of the Hsp90-Binding FKBP Immunophilins

Functions of the Hsp90-Binding FKBP Immunophilins

The Role of Peptidyl Prolyl Isomerases in Aging and Vascular Diseases

The Emerging Role of TPR-Domain Immunophilins in the Mechanism of Action of Steroid Receptors

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