14-3-3 proteins: A historic overview

Aitken, Alastair

doi:10.1016/j.semcancer.2006.03.005

Cited by 739 publications

(767 citation statements)

References 122 publications

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“…It has been shown that 14-3-3 can interact with various proteins and influence the localization of target molecules and/or regulate the enzymatic activity (Aitken, 1995;Fu et al, 2000;Muslin and Xing, 2000;van Hemert et al, 2001;Tzivion and Avruch, 2002;Aitken, 2006). We found that 14-3-3␤ attenuates the phosphatase activity of MLCP, but not the catalytic subunit.…”

Section: Discussionmentioning

confidence: 66%

“…14-3-3 is an acidic small-molecular-mass protein that is widely expressed in a variety of organisms, and it is thought that 14-3-3 play a role in various cellular processes such as signal transduction, cell cycle regulation, apoptosis, and cytoskeletal reorganization (Fu et al, 2000;van Hemert et al, 2001;Tzivion and Avruch, 2002;Aitken, 2006), although the function of 14-3-3 is still not completely understood. Here we report that 14-3-3 binds to MYPT1 and the binding attenuates MLCP phosphatase activity and induces dissociation of MYPT1 from myosin.…”

Section: Introductionmentioning

confidence: 99%

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A Novel Regulatory Mechanism of Myosin Light Chain Phosphorylation via Binding of 14-3-3 to Myosin Phosphatase

Koga

Ikebe

2008

MBoC

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Myosin II phosphorylation–dependent cell motile events are regulated by myosin light-chain (MLC) kinase and MLC phosphatase (MLCP). Recent studies have revealed myosin phosphatase targeting subunit (MYPT1), a myosin-binding subunit of MLCP, plays a critical role in MLCP regulation. Here we report the new regulatory mechanism of MLCP via the interaction between 14-3-3 and MYPT1. The binding of 14-3-3β to MYPT1 diminished the direct binding between MYPT1 and myosin II, and 14-3-3β overexpression abolished MYPT1 localization at stress fiber. Furthermore, 14-3-3β inhibited MLCP holoenzyme activity via the interaction with MYPT1. Consistently, 14-3-3β overexpression increased myosin II phosphorylation in cells. We found that MYPT1 phosphorylation at Ser472 was critical for the binding to 14-3-3. Epidermal growth factor (EGF) stimulation increased both Ser472 phosphorylation and the binding of MYPT1-14-3-3. Rho-kinase inhibitor inhibited the EGF-induced Ser472 phosphorylation and the binding of MYPT1-14-3-3. Rho-kinase specific siRNA also decreased EGF-induced Ser472 phosphorylation correlated with the decrease in MLC phosphorylation. The present study revealed a new RhoA/Rho-kinase–dependent regulatory mechanism of myosin II phosphorylation by 14-3-3 that dissociates MLCP from myosin II and attenuates MLCP activity.

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Section: Discussionmentioning

confidence: 66%

Section: Introductionmentioning

confidence: 99%

A Novel Regulatory Mechanism of Myosin Light Chain Phosphorylation via Binding of 14-3-3 to Myosin Phosphatase

Koga

Ikebe

2008

MBoC

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“…YWHAZ is an oncogene and adapter/scaffold protein needed for cell signaling, cycle control and survival of tumor cells (Aitken, 2006). It is overexpressed in several tumor cells (Morrison, 2009), including MM plasma cells in which it has a possible oncogenic function (Lu et al, 2010).…”

Section: Angiogenic Proteins Of Mmecs S Berardi Et Almentioning

confidence: 99%

Four proteins governing overangiogenic endothelial cell phenotype in patients with multiple myeloma are plausible therapeutic targets

et al. 2011

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Bone marrow (BM) angiogenesis has an important role in the initiation and progression of multiple myeloma (MM). We looked at novel mechanisms of vessel formation in patients with MM through a comparative proteomic analysis between BM endothelial cells (ECs) of patients with active MM (MMECs) and ECs of patients with monoclonal gammopathy of undetermined significance (MGECs) and of subjects with benign anemia (normal ECs). Four proteins were found overexpressed in MMECs: filamin A, vimentin, a-crystallin B and 14-3-3f/d protein, not yet linked to overangiogenic phenotype. These proteins gave a typical distribution in the BM of MM patients and in MMECs versus MGECs, plausibly according to a different functional state. Their expression was enhanced by vascular endothelial growth factor, fibroblast growth factor 2, hepatocyte growth factor and MM plasma cell conditioned medium in step with enhancement of MMEC angiogenesis. Their silencing RNA knockdown affected critical MMEC angiogenesis-related functions, such as spreading, migration and tubular morphogenesis. A gradual stabilization of 14-3-3f/d protein was observed, with transition from normal ECs to MGECs and MMECs that may be a critical step for the angiogenic switch in MMECs and maintenance of the cell overangiogenic phenotype. These proteins were substantially impacted by anti-MM drugs, such as bortezomib, lenalidomide and panobinostat. Results suggest that these four proteins could be new targets for the antiangiogenic management of MM patients.

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“…the 14-3-3 isoform is nearly absent in many tissues, including brain, but expressed at the level of actin in keratinocytes) (8). The 14-3-3 proteins exert their function as homo-or heterodimers (1,2,9), often by binding one or two partners, which are phosphorylated at Ser/Thr residues within specific sequence motifs (10 -12).…”

mentioning

confidence: 99%

“…However, the structure of the regulatory N-terminal domain of TH and TPH2 has not been solved yet, and there is little sequence homology between the 14-3-3-interaction motifs in these hydroxylases and other partners. The phosphorylated 14-3-3-interacting proteins present three main binding motifs, RSXpSXP (mode I), RX(Y/F)XpSXP (mode II) (12), and a carboxyl-terminal (pS/pT)X 1-2 -COOH motif (mode III), where X is not Pro (1). The hydroxylases bind through sequence motifs that do not conform to the I-III consensus binding modes (Fig.…”

mentioning

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

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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.

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14-3-3 proteins: A historic overview

Cited by 739 publications

References 122 publications

A Novel Regulatory Mechanism of Myosin Light Chain Phosphorylation via Binding of 14-3-3 to Myosin Phosphatase

A Novel Regulatory Mechanism of Myosin Light Chain Phosphorylation via Binding of 14-3-3 to Myosin Phosphatase

Four proteins governing overangiogenic endothelial cell phenotype in patients with multiple myeloma are plausible therapeutic targets

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

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