Visualisation of macropinosome maturation by the recruitment of sorting nexins

Kerr, Markus C., Lindsay, Margaret R., Luetterforst, Robert, Hamilton, Nicholas, Simpson, Fiona, Parton, Robert G., Gleeson, Paul A. and Teasdale, Rohan D. (2006) Visualisation of macropinosome maturation by the recruitment of sorting nexins. Journal Of Cell Science, 119 19: 3967-3980. doi:10.1242/jcs.03167

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Author Kerr, Markus C.
Lindsay, Margaret R.
Luetterforst, Robert
Hamilton, Nicholas
Simpson, Fiona
Parton, Robert G.
Gleeson, Paul A.
Teasdale, Rohan D.
Title Visualisation of macropinosome maturation by the recruitment of sorting nexins
Journal name Journal Of Cell Science   Check publisher's open access policy
ISSN 0021-9533
1477-9137
0269-3518
Publication date 2006-10-01
Sub-type Article (original research)
DOI 10.1242/jcs.03167
Open Access Status File (Publisher version)
Volume 119
Issue 19
Start page 3967
End page 3980
Total pages 14
Place of publication Cambridge
Publisher Company Of Biologists
Language eng
Subject C1
270103 Protein Targeting and Signal Transduction
780105 Biological sciences
0601 Biochemistry and Cell Biology
Abstract We report that phosphoinositol-binding sorting nexin 5 ( SNX5) associates with newly formed macropinosomes induced by EGF stimulation. We used the recruitment of GFP-SNX5 to macropinosomes to track their maturation. Initially, GFP-SNX5 is sequestered to discrete subdomains of the macropinosome; these subdomains are subsequently incorporated into highly dynamic, often branched, tubular structures. Time-lapse videomicroscopy revealed the highly dynamic extension of SNX5-labelled tubules and their departure from the macropinosome body to follow predefined paths towards the perinuclear region of the cell, before fusing with early endosomal acceptor membranes. The extension and departure of these tubular structures occurs rapidly over 5-10 minutes and is dependent upon intact microtubules. As the tubular structures depart from the macropinosome there is a reduction in the surface area and an increase in tension of the limiting membrane of the macropinosome. In addition to the recruitment of SNX5 to the macropinosome, Rab5, SNX1 and EEA1 are also recruited by newly formed macropinosomes, followed by the accumulation of Rab7. SNX5 forms heterodimers with SNX1 and this interaction is required for endosome association of SNX5. We propose that the departure of SNX5-positive tubules represents a rapid mechanism of recycling components from macropinosomes thereby promoting their maturation into Rab7-positive structures. Collectively these findings provide a detailed real-time characterisation of the maturation process of the macropinocytic endosome.
Keyword Sorting nexin
Macropinosome
Maturation
Endosomal trafficking
Epidermal-growth-factor
Endosomal Localization
Actin Cytoskeleton
Protein
Transport
Domains
Microtubules
Pinocytosis
Degradation
Involvement
Q-Index Code C1

 
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Created: Wed, 15 Aug 2007, 19:28:34 EST