The University of Southampton
University of Southampton Institutional Repository

Phosphatidylinositol 5 phosphate (Pi5p): From behind the scenes to the front (nuclear) stage

Phosphatidylinositol 5 phosphate (Pi5p): From behind the scenes to the front (nuclear) stage
Phosphatidylinositol 5 phosphate (Pi5p): From behind the scenes to the front (nuclear) stage

Phosphatidylinositol (PI)-related signaling plays a pivotal role in many cellular aspects, including survival, cell proliferation, differentiation, DNA damage, and trafficking. PI is the core of a network of proteins represented by kinases, phosphatases, and lipases which are able to add, remove or hydrolyze PI, leading to different phosphoinositide products. Among the seven known phosphoinositides, phosphatidylinositol 5 phosphate (PI5P) was the last to be discovered. PI5P presence in cells is very low compared to other PIs. However, much evidence collected throughout the years has described the role of this mono-phosphoinositide in cell cycles, stress response, T-cell activation, and chromatin remodeling. Interestingly, PI5P has been found in different cellular compartments, including the nucleus. Here, we will review the nuclear role of PI5P, describing how it is synthesized and regulated, and how changes in the levels of this rare phosphoinositide can lead to different nuclear outputs.

Myotubularin, Nucleus, Phosphatases, PI5P, PI5P4K/PIP4K, PIKFyve
1661-6596
Poli, Alessandro
e856efa4-09b7-41fc-a169-0a1f9eb9bdab
Zaurito, Antonio Enrico
37f44011-f29d-4942-a117-b49486dac6e0
Abdul-Hamid, Shidqiyyah
7703bfce-0078-46ee-a33e-d467fbdca319
Fiume, Roberta
ed01a587-2ca6-480d-baa3-cc221a6830ae
Faenza, Irene
65f048ad-fb3f-4cc5-b4cd-cfc18f9454fd
Divecha, Nullin
5c2ad0f8-4ce7-405f-8a15-2fc4ab96d787
Poli, Alessandro
e856efa4-09b7-41fc-a169-0a1f9eb9bdab
Zaurito, Antonio Enrico
37f44011-f29d-4942-a117-b49486dac6e0
Abdul-Hamid, Shidqiyyah
7703bfce-0078-46ee-a33e-d467fbdca319
Fiume, Roberta
ed01a587-2ca6-480d-baa3-cc221a6830ae
Faenza, Irene
65f048ad-fb3f-4cc5-b4cd-cfc18f9454fd
Divecha, Nullin
5c2ad0f8-4ce7-405f-8a15-2fc4ab96d787

Poli, Alessandro, Zaurito, Antonio Enrico, Abdul-Hamid, Shidqiyyah, Fiume, Roberta, Faenza, Irene and Divecha, Nullin (2019) Phosphatidylinositol 5 phosphate (Pi5p): From behind the scenes to the front (nuclear) stage. International Journal of Molecular Sciences, 20 (9), [2080]. (doi:10.3390/ijms20092080).

Record type: Review

Abstract

Phosphatidylinositol (PI)-related signaling plays a pivotal role in many cellular aspects, including survival, cell proliferation, differentiation, DNA damage, and trafficking. PI is the core of a network of proteins represented by kinases, phosphatases, and lipases which are able to add, remove or hydrolyze PI, leading to different phosphoinositide products. Among the seven known phosphoinositides, phosphatidylinositol 5 phosphate (PI5P) was the last to be discovered. PI5P presence in cells is very low compared to other PIs. However, much evidence collected throughout the years has described the role of this mono-phosphoinositide in cell cycles, stress response, T-cell activation, and chromatin remodeling. Interestingly, PI5P has been found in different cellular compartments, including the nucleus. Here, we will review the nuclear role of PI5P, describing how it is synthesized and regulated, and how changes in the levels of this rare phosphoinositide can lead to different nuclear outputs.

Text
ijms-20-02080 - Version of Record
Available under License Creative Commons Attribution.
Download (591kB)

More information

Accepted/In Press date: 23 April 2019
e-pub ahead of print date: 27 April 2019
Keywords: Myotubularin, Nucleus, Phosphatases, PI5P, PI5P4K/PIP4K, PIKFyve

Identifiers

Local EPrints ID: 431465
URI: http://eprints.soton.ac.uk/id/eprint/431465
ISSN: 1661-6596
PURE UUID: 8f3b7266-9b32-44f1-8c0f-19f6388bc038

Catalogue record

Date deposited: 05 Jun 2019 16:30
Last modified: 07 Oct 2020 01:00

Export record

Altmetrics

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×