Nanoclusters of GPI-Anchored Proteins Are Formed by Cortical Actin-Driven Activity

被引：388

作者：

Goswami, Debanjan ^{[1
]}

Gowrishankar, Kripa ^{[2
]}

Bilgrami, Sameera ^{[1
]}

Ghosh, Subhasri ^{[1
]}

Raghupathy, Riya ^{[1
]}

Chadda, Rahul ^{[1
]}

Vishwakarma, Ram ^{[3
]}

Rao, Madan ^{[1
,2
]}

Mayor, Satyajit ^{[1
]}

机构：

[1] Nat Ctr Biol Sci TIFR, Bangalore 560065, Karnataka, India

[2] Raman Res Inst, Bangalore 560080, Karnataka, India

[3] Natl Inst Immunol, New Delhi 110067, India

来源：

CELL | 2008年 / 135卷 / 06期

关键词：

D O I：

10.1016/j.cell.2008.11.032

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Several cell-surface lipid-tethered proteins exhibit a concentration-independent, cholesterol-sensitive organization of nanoscale clusters and monomers. To understand the mechanism of formation of these clusters, we investigate the spatial distribution and steady-state dynamics of fluorescently tagged GPI-anchored protein nanoclusters using high-spatial and temporal resolution FRET microscopy. These studies reveal a nonrandom spatial distribution of nanoclusters, concentrated in optically resolvable domains. Monitoring the dynamics of recovery of fluorescence intensity and anisotropy, we find that nanoclusters are immobile, and the dynamics of inter-conversion between nanoclusters and monomers, over a range of temperatures, is spatially heterogeneous and non-Arrhenius, with a sharp crossover coinciding with a reduction in the activity of cortical actin. Cholesterol depletion perturbs cortical actin and the spatial scale and interconversion dynamics of nanoclusters. Direct perturbations of cortical actin activity also affect the construction, dynamics, and spatial organization of nanoclusters. These results suggest a unique mechanism of complexation of cell-surface molecules regulated by cortical actin activity.

引用

页码：1085 / 1097

页数：13

共 36 条

[1]

Becker W., 2005, ADV TIME CORRELATED

[2]

Bretscher A, 1997, J CELL SCI, V110, P3011

[3] Cholesterol-sensitive Cdc42 activation regulates actin polymerization for endocytosis via the GEEC pathway [J].

Chadda, Rahul ;

Howes, Mark T. ;

Plowman, Sarah J. ;

Hancock, John F. ;

Parton, Robert G. ;

Mayor, Satyajit .

TRAFFIC, 2007, 8 (06) :702-717

[4]

Chaikin P., 1995, PRINCIPLES CONDENSED

[5] Non-equilibration of hydrostatic pressure in blebbing cells [J].

Charras, GT ;

Yarrow, JC ;

Horton, MA ;

Mahadevan, L ;

Mitchison, TJ .

NATURE, 2005, 435 (7040) :365-369

[6] Life and times of a cellular bleb [J].

Charras, Guillaume T. ;

Coughlin, Margaret ;

Mitchison, Timothy J. ;

Mahadevan, L. .

BIOPHYSICAL JOURNAL, 2008, 94 (05) :1836-1853

[7] Reassembly of contractile actin cortex in cell blebs [J].

Charras, Guillaume T. ;

Hu, Chi-Kuo ;

Coughlin, Margaret ;

Mitchison, Timothy J. .

JOURNAL OF CELL BIOLOGY, 2006, 175 (03) :477-490

[8] GPI anchoring leads to sphingolipid-dependent retention of endocytosed proteins in the recycling endosomal compartment [J].

Chatterjee, S ;

Smith, ER ;

Hanada, K ;

Stevens, VL ;

Mayor, S .

EMBO JOURNAL, 2001, 20 (07) :1583-1592

[9] Transient anchorage of cross-linked glycosyl-phosphatidylinositol-anchored proteins depends on cholesterol, Src family kinases, caveolin, and phosphoinositides [J].

Chen, Yun ;

Thelin, William R. ;

Yang, Bing ;

Milgram, Sharon L. ;

Jacobson, Ken .

JOURNAL OF CELL BIOLOGY, 2006, 175 (01) :169-178

[10] The many faces of actin: Matching assembly factors with cellular structures [J].

Chhabra, Ekta Seth ;

Higgs, Henry N. .

NATURE CELL BIOLOGY, 2007, 9 (10) :1110-1121

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