Related Experiment Video
Updated: Aug 15, 2026
12:58
Expression of Exogenous Cytokine in Patient-derived Xenografts via Injection with a Cytokine-transduced Stromal Cell Line
Published on: May 10, 2017
SHIP, a new player in cytokine-induced signalling
1Terry Fox Laboratory, British Columbia Cancer Research Centre, Vancouver, Canada.
Leukemia
|February 1, 1997
Summary
A novel inositol polyphosphate 5-phosphatase (5-ptase), named SHIP, was identified. This enzyme plays a key role in cell signaling pathways, influencing proliferation, differentiation, and apoptosis.
Area of Science:
- Molecular Biology
- Cell Signaling
- Biochemistry
Background:
- Novel 145 kDa inositol polyphosphate 5-phosphatase (5-ptase) identified in murine and human cells.
- This enzyme is tyrosine phosphorylated and associates with Shc upon cytokine stimulation of hemopoietic cells.
Purpose of the Study:
- To review the cloning, Shc binding, and functional role of the novel 5-ptase, SH2-containing inositol 5-phosphatase (SHIP).
- To elucidate SHIP's involvement in cell proliferation, differentiation, and apoptosis.
Main Methods:
- Purification and cDNA cloning of murine and human SHIP.
- Analysis of substrate specificity, distinguishing it from other 5-ptases.
- Investigation of tyrosine phosphorylation and Shc association.
Main Results:
- SHIP selectively hydrolyzes inositol-1,3,4,5-tetraphosphate (I-1,3,4,5-P4) and phosphatidylinositol-3,4,5-trisphosphate (PI-3,4,5-P3).
- SHIP possesses a unique SH2 domain, differentiating it from other 5-ptases.
- SHIP is implicated in growth factor-mediated signaling pathways.
Conclusions:
- SHIP is a unique enzyme with a critical role in regulating cell signaling.
- SHIP's SH2 domain and substrate specificity suggest a significant function in cell proliferation, differentiation, and apoptosis.
More Related Videos
Related Concept Videos
01:24Intracellular Signaling Cascades
Once a ligand binds to a receptor, the signal is transmitted through the membrane and into the cytoplasm. The continuation of a signal in this manner is called signal transduction. Signal transduction only occurs with cell-surface receptors, which cannot interact with most components of the cell, such as DNA. Only internal receptors can interact directly with DNA in the nucleus to initiate protein synthesis. When a ligand binds to its receptor, conformational changes occur that affect the...
01:30Assembly of Signaling Complexes
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
01:15Amplifying Signals via Second Messengers
Many receptor binding ligands are hydrophilic; they do not cross the cell membrane but bind to cell-surface receptors. Thus, their message must be relayed by second messengers present in the cell cytoplasm. There are several second messenger pathways, each with its own way of relaying information. For example, the G protein-coupled receptors can activate both phosphoinositol and cyclic AMP (cAMP) second messenger pathways. The phosphoinositol pathway is active when the receptor induces...
01:22Amplifying Signals via Enzymatic Cascade
When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...
01:20The JAK-STAT Signaling Pathway
Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as SH2...
01:17Intracellular Signaling Affects Focal Adhesions
Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Some...