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A novel probe for phosphatidylinositol 4-phosphate reveals multiple pools beyond the Golgi

Hammond, Gerald R.V., Machner, Matthias P., Balla, Tamas·2014·Journal of Cell Biology
DOI 10.1083/jcb.201312072PMC PMC3987136
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Abstract

Polyphosphoinositides are an important class of lipid that recruit specific effector proteins to organelle membranes. One member, phosphatidylinositol 4-phosphate (PtdIns4P) has been localized to Golgi membranes based on the distribution of lipid binding modules from PtdIns4P effector proteins. However, these probes may be biased by additional interactions with other Golgi-specific determinants. In this paper, we derive a new PtdIns4P biosensor using the PtdIns4P binding of SidM (P4M) domain of the secreted effector protein SidM from the bacterial pathogen Legionella pneumophila. PtdIns4P was necessary and sufficient for localization of P4M, which revealed pools of the lipid associated not only with the Golgi but also with the plasma membrane and Rab7-positive late endosomes/lysosomes. PtdIns4P distribution was determined by the localization and activities of both its anabolic and catabolic enzymes. Therefore, P4M reports a wider cellular distribution of PtdIns4P than previous probes and therefore will be valuable for dissecting the biological functions of PtdIns4P in its assorted membrane compartments.

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Cited by

Sorted by citations

Metadata

Authors
Hammond, G. R. V., Machner, M. P., & Balla, T.
Affiliations
Program in Developmental Neuroscience 1 and 2
Venue
Journal of Cell Biology
Publisher
Rockefeller University Press
Published
2014-04-07
Volume
205
Issue
1
Pages
113-126
ISSN
  • 1540-8140
  • 0021-9525
DOI
10.1083/jcb.201312072
PMC
PMC3987136
Cited by
453
References
2
Language
en

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