Targeted Proteomic Analysis of 14-3-3ς, a p53 Effector Commonly Silenced in Cancer

Benzinger, Anne; Muster, Nemone; Koch, Heike; Yates, John R.; Hermeking, Heiko

doi:10.1074/mcp.m500021-mcp200

Cited by 171 publications

(153 citation statements)

References 45 publications

(44 reference statements)

Supporting

Mentioning

138

Contrasting

Unclassified

Order By: Relevance

“…In contrast to Du et al (16), Snail1 phosphorylation at Ser-11 did not affect nucleocytoplasmic shuttling of the protein. This may be explained by 14-3-3 down-regulation in many tumor cells by different mechanisms (39) including promotor methylation and inhibition downstream of p53 mutations, thereby facilitating cancer formation by many routes (40). Indeed, PKD1KD was not able to induce nuclear localization of primarily cytoplasmic Snail1 in non-transformed, immortalized HEK293T cells (supplemental Fig.…”

Section: Discussionmentioning

confidence: 99%

Protein Kinase D1 Mediates Anchorage-dependent and -independent Growth of Tumor Cells via the Zinc Finger Transcription Factor Snail1

Eiseler

Köhler

Nimmagadda

et al. 2012

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background:The protein kinase D (PKD) family is involved in the control of cell motility and proliferation. Results: PKD1 controls growth of cancer cells through phosphorylation of Snail1 at Ser-11. Conclusion: Only PKD1, but not PKD2, mediates isoform-specific control of pancreatic cancer cell proliferation through Snail1. Significance: We demonstrate for the first time isoform-specific control of pancreatic cancer growth by a single phosphorylation of a substrate.

show abstract

Section: Discussionmentioning

confidence: 99%

Protein Kinase D1 Mediates Anchorage-dependent and -independent Growth of Tumor Cells via the Zinc Finger Transcription Factor Snail1

Eiseler

Köhler

Nimmagadda

et al. 2012

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…We recently used a targeted proteomics approach to identify 14-3-3σ-associated proteins in vivo [30]. Interestingly, we found that in colorectal cancer cells 14-3-3σ was only present as a homo-dimer or as a hetero-dimer with 14-3-3γ indicating selective dimerization, which may be due to the putative dimerization determinants identified here [30]. The data presented here provides a basis for the experimental validation of determinants of ligand and dimerization specificity by mutational analysis.…”

Section: Figmentioning

confidence: 99%

The crystal structure of the non-liganded 14-3-3σ protein: insights into determinants of isoform specific ligand binding and dimerization

et al. 2005

Self Cite

View full text Add to dashboard Cite

show abstract

“…hTH1 (0.05 M) was preincubated for 4 min at 30°C in 40 mM NaHepes, pH 7.0, with 25 M L-Tyr, 0.05 mg/ml catalase, 30 M Fe(II)SO 4 , and, when indicated, 1.8 M 14-3-3 (␥ or ). The samples were then further incubated 4 min at 30°C in the absence or presence of liposomes made of PC:PBPS:SDPS: DPPC (20 M phospholipid concentration).…”

Section: Methodsmentioning

confidence: 99%

Three-way Interaction between 14-3-3 Proteins, the N-terminal Region of Tyrosine Hydroxylase, and Negatively Charged Membranes

Halskau

Ying

Baumann

et al. 2009

Journal of Biological Chemistry

View full text Add to dashboard Cite

Tyrosine hydroxylase (TH), the rate-limiting enzyme in the synthesis of catecholamines, is activated by phosphorylationdependent binding to 14-3-3 proteins. The N-terminal domain of TH is also involved in interaction with lipid membranes. We investigated the binding of the N-terminal domain to its different partners, both in the unphosphorylated (TH-(1-43)) and Ser 19 -phosphorylated (THp-(1-43)) states by surface plasmon resonance. THp-(1-43) showed high affinity for 14-3-3 proteins (K d ϳ 0.5 M for 14-3-3␥ and -and 7 M for 14-3-3 ). The domains also bind to negatively charged membranes with intermediate affinity (concentration at half-maximal binding S 0.5 ‫؍‬ 25-58 M (TH-(1-43)) and S 0.5 ‫؍‬ 135-475 M (THp-(1-43)), depending on phospholipid composition) and concomitant formation of helical structure. 14-3-3␥ showed a preferential binding to membranes, compared with 14-3-3 , both in chromaffin granules and with liposomes at neutral pH. The affinity of 14-3-3␥ for negatively charged membranes (S 0.5 ‫؍‬ 1-9 M) is much higher than the affinity of TH for the same membranes, compatible with the formation of a ternary complex between Ser 19 -phosphorylated TH, 14-3-3␥, and membranes. Our results shed light on interaction mechanisms that might be relevant for the modulation of the distribution of TH in the cytoplasm and membrane fractions and regulation of L-DOPA and dopamine synthesis.

show abstract

Targeted Proteomic Analysis of 14-3-3ς, a p53 Effector Commonly Silenced in Cancer

Cited by 171 publications

References 45 publications

Protein Kinase D1 Mediates Anchorage-dependent and -independent Growth of Tumor Cells via the Zinc Finger Transcription Factor Snail1

Protein Kinase D1 Mediates Anchorage-dependent and -independent Growth of Tumor Cells via the Zinc Finger Transcription Factor Snail1

The crystal structure of the non-liganded 14-3-3σ protein: insights into determinants of isoform specific ligand binding and dimerization

Three-way Interaction between 14-3-3 Proteins, the N-terminal Region of Tyrosine Hydroxylase, and Negatively Charged Membranes

Contact Info

Product

Resources

About