Phosphoinositides and Downstream Signalling Molecules
A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biology".
Deadline for manuscript submissions: closed (31 July 2020) | Viewed by 42228
Special Issue Editors
Interests: lipid metabolism; gastrointestinal diseases; pancreatic cancer; extracellular vesicles; tumour-stroma crosstalk; cannabinoid signalling
Special Issues, Collections and Topics in MDPI journals
Interests: signal transduction; prostate and skin cancers; phosphoinositide signalling; phosphoinositide 3-kinases-dependent pathways
Special Issues, Collections and Topics in MDPI journals
Special Issue Information
Dear Colleagues,
Phosphoinositides (PIs) are phospholipids comprising a water-soluble myo-inositol head group linked to two fatty acid chains by a glycerol moiety. The enzyme phosphatidylinositol (PtdIns) catalyses the synthesis of the founding member of the family, PtdIns, by linking the 1-position of the myo-inositol to the diester phosphate of a glycerophospholipid. PIs derive from differential phosphorylation of the hydroxyls at the 3-, 4- and 5-position within the myo-inositol headgroup of PtdIns. All seven PIs are naturally occurring in all higher eukaryotes, and their levels can be modified by the action of specific kinases or phosphatases. Because of their lipid tail, PIs are obligatorily membrane-bound; therefore, they can mark specific membrane compartments, or subdomains within a membrane. On the other hand, PIs can also act as signalling molecules, either by modulating activation of target proteins or by acting as precursors of other, “PIs-derived”, signalling molecules such as lysophosphatidylinositol and inositol phosphates. This Special Issue will provide an overview of the long journey of PIs and their downstream signalling molecules from mere cellular components to their identification as key regulators of several cellular signalling, including the most recent evidence reporting several intracellular roles for the least investigated members of this family.
Prof. Dr. Marco Falasca
Dr. Tania Maffucci
Guest Editors
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Keywords
- phosphoinositides
- inositol phosphates
- lysophosphatidylinositol
- PI-binding domains
- PI-kinases
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