p23, a simple protein with complex activities

Felts, Sara J.; Toft, David O.

doi:10.1379/1466-1268(2003)008<0108:paspwc>2.0.co;2

Cited by 105 publications

(88 citation statements)

References 38 publications

(60 reference statements)

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“…Hsp90 is a highly conserved molecular chaperone essential for activating many signaling proteins in eukaryotic cells (32). The Hsp90 cochaperone p23 appears to directly interact with ATP-bound form of Hsp90 and promote the maturation of client proteins (26). p23 is also found to stabilize the client protein-Hsp90 complex in vivo (33).…”

Section: Discussionmentioning

confidence: 99%

“…p23 is also found to stabilize the client protein-Hsp90 complex in vivo (33). Even though the proteins containing the p23_like domain, the core-folding motif of p23 protein may have diverse functions, most of them seem to associate with Hsp90 (25,26). For example, Sgt1p, a conserved protein with the p23_like domain, has been found to act as an adaptor protein that recruits specific client proteins to Hsp90 complex by binding to both Hsp90 and its client proteins (27).…”

Section: Discussionmentioning

confidence: 99%

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NudC-like protein 2 regulates the LIS1/dynein pathway by stabilizing LIS1 with Hsp90

Yang

Yan²,

Cai³

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

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The type I lissencephaly gene product LIS1, a key regulator of cytoplasmic dynein, is critical for cell proliferation, survival, and neuronal migration. However, little is known about the regulation of LIS1. Here, we identify a previously uncharacterized mammalian homolog of Aspergillus NudC, NudCL2 (NudC-like protein 2), as a regulator of LIS1. NudCL2 is localized to the centrosome in interphase, and spindle poles and kinetochores during mitosis, a pattern similar to the localization of LIS1 and cytoplasmic dynein. Depletion of NudCL2 destabilized LIS1 and led to phenotypes resembling those of either dynein or LIS1 deficiency. NudCL2 complexed with and enhanced the interaction between LIS1 and Hsp90. Either disruption of the LIS1-Hsp90 interaction with the C terminus of NudCL2 or inhibition of Hsp90 chaperone function by geldanamycin decreased LIS1 stability. Thus, our results suggest that NudCL2 regulates the LIS1/dynein pathway by stabilizing LIS1 with Hsp90 chaperone. This represents a hitherto undescribed mechanism of the LIS1/dynein regulation in mammalian cells.cochaperone | heat shock protein 90 | lissencephaly 1 | migration | p23

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

NudC-like protein 2 regulates the LIS1/dynein pathway by stabilizing LIS1 with Hsp90

Yang

Yan²,

Cai³

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

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“…2, Table 2), the highest number of them corresponding to genes encoding hypothetical proteins and genes that had no matches in databases. The other probe sets corresponded to genes encoding a 40S ribosomal protein, related to translation, and a protein homologous to the translationally controlled tumour protein (TCTP), also called fortilin or P23, a protein with chaperoning activity related to mitotic proliferation during the early stages of cell differentiation (Felts & Toft, 2003). TCTP/P23 overexpression in human cells leads to cell elongation resembling hyphal growth in fungi.…”

Section: Overview Of the Trichoderma Gene Expression Data From Microamentioning

confidence: 99%

Comparative study of Trichoderma gene expression in interactions with tomato plants using high-density oligonucleotide microarrays

et al. 2012

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Trichoderma spp. are widely used as biopesticides and biofertilizers to control diseases and to promote positive physiological responses in plants. In vitro and in vivo assays with Trichoderma harzianum CECT 2413 (T34), Trichoderma virens Gv29-8 (T87) and Trichoderma hamatum IMI 224801 (T7) revealed that these strains affected the growth and development of lateral roots in tomato plants in different ways. The early expression profiles of these Trichoderma strains were studied after 20 h of incubation in the presence of tomato plants, using a high-density oligonucleotide (HDO) microarray, and compared to the profiles in the absence of plants. Out of the total 34 138 Trichoderma probe sets deposited on the microarray, 1077 (3.15 %) showed a significant change of at least 2-fold in expression in the presence of tomato plants. The numbers of probe sets identified in the individual Trichoderma strains were 593 in T. harzianum T34, 336 in T. virens T87 and 94 in T. hamatum T7. Carbohydrate metabolism -the chitin degradation enzymes N-acetylglucosamine-6-phosphate deacetylase, glucosamine-6-phosphate deaminase and chitinase -was the most significantly overrepresented process commonly observed in the three Trichoderma strains in early interactions with tomato plants. Strains T7 and T34, which had similar positive effects on plant development in biological assays, showed a significantly overrepresented hexokinase activity in interaction with tomato. In addition, genes encoding a 40S ribosomal protein and a P23 tumour protein were altered in both these strains.

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“…The p23-HSP90 protein complex is involved in the assembly of steroid hormone receptor and telomerase complexes, and also regulates the binding, folding and processing of proteins. 9,10 We assessed the expression of p23 in cell extracts isolated from untreated and ER stress-induced cells. As shown in Figure 2, p23 is a low molecular weight (23 kD) chaperone protein whose expression is detectable both in MCF-7 and Apaf-1 À/À fibroblasts.…”

Section: Hsp90 Protein Expression Patterns In Different Cell Linesmentioning

confidence: 99%

Coupling endoplasmic reticulum stress to the cell-death program: a novel HSP90-independent role for the small chaperone protein p23

et al. 2005

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The endoplasmic reticulum (ER) is the principal organelle for the biosynthesis of proteins, steroids and many lipids, and is highly sensitive to alterations in its environment. Perturbation of Ca 2 þ homeostasis, elevated secretory protein synthesis, deprivation of glucose or other sugars, altered glycosylation and/or the accumulation of misfolded proteins may all result in ER stress, and prolonged ER stress triggers cell death. Studies from multiple laboratories have identified the roles of several ER stress-induced cell-death modulators and effectors through the use of biochemical, pharmacological and genetic tools. In the present work, we describe the role of p23, a small chaperone protein, in preventing ER stress-induced cell death. p23 is a highly conserved chaperone protein that modulates HSP90 activity and is also a component of the steroid receptors. p23 is cleaved during ER stress-induced cell death; this cleavage, which occurs close to the carboxy-terminus, requires caspase-3 and/or caspase-7, but not caspase-8. Blockage of the caspase cleavage site of p23 was associated with decreased cell death induced by ER stress. Immunodepletion of p23 or inhibition of p23 expression by siRNA resulted in enhancement of ER stress-induced cell death. While p23 co-immunoprecipitated with the BH3-only protein PUMA (p53-upregulated modulator of apoptosis) in untreated cells, prolonged ER stress disrupted this interaction. The results define a protective role for p23, and provide further support for a model in which ER stress is coupled to the mitochondrial intrinsic apoptotic pathway through the activities of BH3 family proteins.

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p23, a simple protein with complex activities

Cited by 105 publications

References 38 publications

NudC-like protein 2 regulates the LIS1/dynein pathway by stabilizing LIS1 with Hsp90

NudC-like protein 2 regulates the LIS1/dynein pathway by stabilizing LIS1 with Hsp90

Comparative study of Trichoderma gene expression in interactions with tomato plants using high-density oligonucleotide microarrays

Coupling endoplasmic reticulum stress to the cell-death program: a novel HSP90-independent role for the small chaperone protein p23

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