The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Phosphoinositides in Constitutive Membrane Traffic
Abstract
Proteins that make, consume, and bind to phosphoinositides are important for constitutive membrane traffic. Different phosphoinositides are concentrated in different parts of the central vacuolar pathway, with phosphatidylinositol 4-phosphate predominate on Golgi, phosphatidylinositol 4,5-bisphosphate predominate at the plasma membrane, phosphatidylinositol 3-phosphate the major phosphoinositide on early endosomes, and phosphatidylinositol 3,5-bisphosphate found on late endocytic organelles. This spatial segregation may be the mechanism by which the direction of membrane traffic is controlled. Phosphoinositides increase the affinity of membranes for peripheral membrane proteins that function for sorting protein cargo or for the docking and fusion of transport vesicles. This implies that constitutive membrane traffic may be regulated by the mechanisms that control the activity of the enzymes that produce and consume phosphoinositides. Although the lipid kinases and phosphatases that function in constitutive membrane traffic are beginning to be identified, their regulation is poorly understood.
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Phosphoinositides in cell regulation and membrane dynamics
Di Paolo, G., & De Camilli, P. (2006) · Nature · doi:10.1038/nature05185 · Cited by 2,790
The intracellular trafficking pathway of transferrin
Mayle, K. M., Le, A. M., & Kamei, D. T. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.09.009 · Cited by 466
A novel probe for phosphatidylinositol 4-phosphate reveals multiple pools beyond the Golgi
Hammond, G. R. V., Machner, M. P., & Balla, T. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201312072 · Cited by 453
Phosphoinositides Regulate Ciliary Protein Trafficking to Modulate Hedgehog Signaling
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How the Ciliary Membrane Is Organized Inside-Out to Communicate Outside-In
Garcia, G., Raleigh, D. R., & Reiter, J. F. (2018) · Current Biology · doi:10.1016/j.cub.2018.03.010 · Cited by 162
Metadata
- Authors
- Roth, M. G.
- Venue
- Physiological Reviews
- Publisher
- American Physiological Society
- Published
- 2004-07
- Volume
- 84
- Issue
- 3
- Pages
- 699-730
- ISSN
- 0031-9333 (ISSN-L)
- 1522-1210
- OpenAlex
- W2147532748
- Cited by
- 297
- References
- 13
- FWCI
- 1.58
- Type
- journal article
- Language
- en
- Open access
- closed
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