Phosphoproteome is the whole complement of phosphorylated proteins in a cell, tissue or organism, and has become an interesting study subject since the discovery of phosphorylation as a key regulatory mechanism of cell life. Phosphoproteomics is a method which studies the compact of the phosphorylated proteins, expression and modification, interaction and association, rule of the regulatory and so on. Recently, phosphoproteomics is widely used in cancer research. It will provide important information in cancer research, cancer diagnosis, and therapy.
ErbB Receptors ; genetics ; Humans ; Neoplasms ; genetics ; metabolism ; Phosphoproteins ; genetics ; metabolism ; Phosphorylation ; Proteomics ; methods ; Signal Transduction

Electrocardiography ; Humans ; Mutation ; Phosphorylation ; Ryanodine Receptor Calcium Release Channel/genetics* ; Tachycardia, Ventricular/genetics*

The 26S proteasome at the center of the ubiquitin-proteasome system (UPS) is essential for virtually all cellular processes of eukaryotes. A common misconception about the proteasome is that, once made, it remains as a static and uniform complex with spontaneous and constitutive activity for protein degradation. Recent discoveries have provided compelling evidence to support the exact opposite insomuch as the 26S proteasome undergoes dynamic and reversible phosphorylation under a variety of physiopathological conditions. In this review, we summarize the history and current understanding of proteasome phosphorylation, and advocate the idea of targeting proteasome kinases/phosphatases as a new strategy for clinical interventions of several human diseases.
Animals ; Humans ; Phosphoprotein Phosphatases ; genetics ; metabolism ; Phosphorylation ; genetics ; Proteasome Endopeptidase Complex ; genetics ; metabolism ; Protein Kinases ; genetics ; metabolism

Animals ; Humans ; Models, Biological ; Oxidative Stress ; genetics ; physiology ; Phosphorylation ; Protein Kinase C ; genetics ; metabolism ; physiology ; Signal Transduction ; genetics ; physiology

Animals ; Eukaryotic Initiation Factors ; genetics ; metabolism ; Humans ; Phosphorylation ; physiology ; Proteomics ; Ribosomal Proteins ; genetics ; metabolism ; TOR Serine-Threonine Kinases ; genetics ; metabolism

Abiotic stresses substantially affect the growth and development of plants. Plants have evolved multiple strategies to cope with the environmental stresses, among which transcription factors play an important role in regulating the tolerance to abiotic stresses. Basic leucine zipper transcription factors (bZIP) are one of the largest gene families. The stability and activity of bZIP transcription factors could be regulated by different post-translational modifications (PTMs) in response to various intracellular or extracellular stresses. This paper introduces the structural feature and classification of bZIP transcription factors, followed by summarizing the PTMs of bZIP transcription factors, such as phosphorylation, ubiquitination and small ubiquitin-like modifier (SUMO) modification, in response to abiotic stresses. In addition, future perspectives were prospected, which may facilitate cultivating excellent stress-resistant crop varieties by regulating the PTMs of bZIP transcription factors.
Basic-Leucine Zipper Transcription Factors/genetics* ; Protein Processing, Post-Translational ; Phosphorylation ; Transcription Factors/genetics* ; Stress, Physiological/genetics*

Timely cell cycle regulation is conducted by sequential activation of a family of serine-threonine kinases called cycle dependent kinases (CDKs). Tight CDK regulation involves cyclin dependent kinase inhibitors (CKIs) which ensure the correct timing of CDK activation in different phases of the cell cycle. One CKI of importance is p27(KIP1). The regulation and cellular localization of p27(KIP1) can result in biologically contradicting roles when found in the nucleus or cytoplasm of both normal and tumor cells. The p27(KIP1) protein is mainly regulated by proteasomal degradation and its downregulation is often correlated with poor prognosis in several types of human cancers. The protein can also be functionally inactivated by cytoplasmic localization or by phosphorylation. The p27(KIP1) protein is an unconventional tumor suppressor because mutation of its gene is extremely rare in tumors, implying the normal function of the protein is deranged during tumor development. While the tumor suppressor function is mediated by p27(KIP1)'s inhibitory interactions with the cyclin/CDK complexes, its oncogenic function is cyclin/CDK independent, and in many cases correlates with cytoplasmic localization. Here we review the basic features and novel aspects of the p27(KIP1) protein, which displays genetically separable tumor suppressing and oncogenic functions.
Animals ; Cyclin-Dependent Kinases/genetics/*metabolism ; Humans ; Intracellular Signaling Peptides and Proteins/genetics/*metabolism ; Mutation ; Neoplasms/genetics/*metabolism ; Phosphorylation/genetics ; Protein Transport/genetics ; Tumor Suppressor Proteins/genetics/*metabolism

Animals ; DNA, Fungal ; Phosphorylation ; RNA Polymerase II ; Sequence Homology, Nucleic Acid ; T-Box Domain Proteins ; genetics

BACKGROUNDRecent studies on bone have shown an endocrine role of the skeleton, which could be impaired in various human diseases, including osteoporosis, obesity, and diabetes-associated bone diseases. As a sensor and regulator of energy metabolism, AMP-activated protein kinase (AMPK) may also play an important role in the regulation of bone metabolism. The current study aimed to establish the expression profiles and phosphorylation patterns of AMPK subunits in several mesenchymal cell types.

METHODSReverse transcription-polymerase chain reaction (PCR) for relative quantification, real-time PCR for absolute quantification, and Western blotting were used to investigate the gene expression profiles and phosphorylation patterns of AMPK subunits in several mesenchymal cell types, including primary human mesenchymal stem cells (hMSCs) and hFOB, Saos-2, C3H/10T1/2, MC3T3-E1, 3T3-L1, and C2C12 cells.

RESULTSAMPKα1 and AMPKβ1 mRNAs were abundantly expressed in all cell types. AMPKγ1 mRNA was abundantly expressed in C3H/10T1/2, MC3T3-E1, 3T3-L1, and C2C12 but not detected in human-derived cell types. AMPKγ2 mRNA was mildly expressed in all cell types. AMPKα1 protein was highly expressed in all cell types and AMPKα2 protein was highly expressed only in hFOB and Saos-2 cells. AMPKβ1 protein was abundantly expressed in all cell types except for Saos-2, in which AMPKβ2 protein overwhelmed AMPKβ1 expression. AMPKγ1 and AMPKγ2 proteins were expressed in C3H/10T1/2, MC3T3-E1, 3T3-L1, and C2C12 cells and only AMPKγ2 protein was expressed in hMSCs, hFOB and Saos-2 cells. AMPKα was phosphorylated at Thr172 and Ser485 and AMPKβ1 was phosphorylated at Ser108 and Ser182 in all cell types with a specific pattern in each cell type.

CONCLUSIONThe combination of AMPK α, β, and γ subunits and phosphorylation of AMPKα (Thr172 and Ser485) and AMPKβ1 (Ser108 and Ser182) showed a specific pattern in each cell type.

AMP-Activated Protein Kinases ; genetics ; metabolism ; Animals ; Cell Line ; Humans ; Mesenchymal Stromal Cells ; enzymology ; Mice ; Phosphorylation

Acetylation ; Animals ; Humans ; Phosphorylation ; Tumor Suppressor Protein p53 ; chemistry ; genetics ; metabolism ; physiology