What is a Phosphodegron?

What is a Phosphodegron?

A phosphodegron is defined as one or a series of phosphorylated residues on the substrate that directly interact with a protein–protein interaction domain in an E3 Ub-ligase (e.g. an F-box protein), thereby linking the substrate to the conjugation machinery (Winston et al., 1999c; Nash et al., 2001).

What is APC in cell biology?

Anaphase-promoting complex (APC) is a one of ubiquitin ligases, which plays a key role in the cell cycle [1]. APC is mainly required to induce progression and exit from mitosis by inducing proteolysis of different cell cycle regulators.

Do all proteins have Degrons?

In fact, some proteins can even contain multiple degrons. Degrons are present in a variety of organisms, from the N-degrons (see N-end Rule) first characterized in yeast to the PEST sequence of mouse ornithine decarboxylase. Degrons have been identified in prokaryotes as well as eukaryotes.

Is ubiquitin a Degron?

The degron The ubiquitin modification delivers the substrate to the proteasome and the unstructured region is the site at which degradation initiates11. Typically both parts of the degron are present in the same protein.

What is the main function of APC?

The APC protein acts as a tumor suppressor, which means that it keeps cells from growing and dividing too fast or in an uncontrolled way. It helps control how often a cell divides, how it attaches to other cells within a tissue, and whether a cell moves within or away from a tissue.

What is the target of APC?

It is well established that APC/C is a target of the SAC (spindle assembly checkpoint) during mitosis and has critical roles in controlling the protein levels of major regulators of mitosis and DNA replication.

How do Degrons work?

A degron is a portion of a protein that is important in regulation of protein degradation rates. Known degrons include short amino acid sequences, structural motifs and exposed amino acids (often Lysine or Arginine) located anywhere in the protein. In fact, some proteins can even contain multiple degrons.

What is proteolysis meaning?

proteolysis, Process in which a protein is broken down partially, into peptides, or completely, into amino acids, by proteolytic enzymes, present in bacteria and in plants but most abundant in animals.

Is proteasome membrane bound?

(b) Proteasome subunits are tightly bound to membranes. Neuronal cultures at DIV14 were fractionated into cytosolic, peripherally-associated (Periph), and tightly-bound (Bound) proteins.

How is anaphase regulated?

Ubiquitin-dependent degradation of cell cycle factors induced by the APC is a key mechanism used by the cell to tightly regulate different transitions throughout cell division. Thus, the APC orchestrates mitosis by controlling anaphase entry, anaphase progression, exit of mitosis and G1 phase.

What is APC testing?

A compilation of material describing what bacteria the Aerobic Plate Count analysis detects and what the results mean. The Aerobic Plate Count (APC) is used as an indicator of bacterial populations on a sample. It is also called the aerobic colony count, standard plate count, Mesophilic count or Total Plate Count.

What is the main function of APC complex?

The anaphase promoting complex or cyclosome (APC/C) is a multi-subunit cullin-RING E3 ubiquitin ligase that functions to regulate progression through the mitotic phase of the cell cycle and to control entry into S phase [1–4].

Does Skp2 play a proto-oncogenic role in cancer progression?

Overexpression of Skp2 is frequently observed in human cancer progression and metastasis, and evidence suggests that Skp2 plays a proto-oncogenic role both in vitro and in vivo. Skp2 overexpression has been seen in: lymphomas, prostate cancer, melanoma, nasopharyngeal carcinoma, pancreatic cancer, and breast carcinomas.

What is the pro-tumor property of Skp2?

Using genetic mouse models and in vitrocell models, the pro-tumor property of Skp2 has been comprehensively demonstrated including cell cycle promotion, cellular senescence and apoptosis prevention, cell migration enhancement, stemness maintenance and many others.

How does Skp2 bind to cyclin E?

The F-box protein SKP2 binds to the phosphorylated threonine 380 in cyclin E and regulates ubiquitin-dependent degradation of cyclin E Biochemical and biophysical research communications, 281(4)(2001), pp. 884-890

What is the role of Skp2 in SCF complex?

In this SCF complex, Skp2 acts as the substrate recognition factor. The F-box proteins are divided into three classes: Fbxws containing WD40 repeat domains, Fbxls containing leucine-rich repeats, and Fbxos containing either different protein–protein interaction modules or no recognizable motifs.