What question did this study set out to answer?

To investigate the structural organization, coalescence behavior, and lipid-driven segregation of raft and non-raft domains in the plasma membrane of non-polarized cells.

May 18, 1998The Journal of Cell BiologyOpen Access

Lipid Domain Structure of the Plasma Membrane Revealed by Patching of Membrane Components

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Authors

THThomas HarderRobert Koch Institute PSPeter ScheiffeleUniversity of Basel PVPaul VerkadeUniversity of Pisa

Discussion

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Overview

In vitro cell study demonstrates segregation of lipid raft and non-raft membrane domains via component patching, suggesting lipid phase immiscibility organizes membrane structure.

Key Points

To investigate the structural organization, coalescence behavior, and lipid-driven segregation of raft and non-raft domains in the plasma membrane of non-polarized cells.
Cross-linked pairs of raft markers (GPI-anchored proteins PLAP and Thy-1, influenza hemagglutinin, ganglioside GM1) and non-raft markers (transferrin receptor) in BHK and Jurkat T-lymphoma cells using antibodies or cholera toxin.
Assessed patching overlap, cytoplasmic recruitment of the src-like tyrosine kinase Fyn, and the effects of cholesterol depletion on domain segregation.
Cross-linked raft markers co-localized extensively and accumulated cytoplasmic Fyn kinase, whereas raft patches segregated sharply from non-raft transferrin receptor patches.
Cholesterol depletion abrogated the spatial segregation between raft and non-raft components, demonstrating that domain separation relies on lipid phase immiscibility.

Cite This Study

Harder et al. (1998) studied this question.

synapsesocial.com/papers/6a6f1899abc331a858078947 https://doi.org/10.1083/jcb.141.4.929

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May 18, 1998The Journal of Cell BiologyOpen Access

Lipid Domain Structure of the Plasma Membrane Revealed by Patching of Membrane Components

View Full Paper

Ask AI

Bookmark

Authors

THThomas HarderRobert Koch Institute PSPeter ScheiffeleUniversity of Basel PVPaul VerkadeUniversity of Pisa

Discussion

Member takes

Overview

In vitro cell study demonstrates segregation of lipid raft and non-raft membrane domains via component patching, suggesting lipid phase immiscibility organizes membrane structure.

Key Points

To investigate the structural organization, coalescence behavior, and lipid-driven segregation of raft and non-raft domains in the plasma membrane of non-polarized cells.
Cross-linked pairs of raft markers (GPI-anchored proteins PLAP and Thy-1, influenza hemagglutinin, ganglioside GM1) and non-raft markers (transferrin receptor) in BHK and Jurkat T-lymphoma cells using antibodies or cholera toxin.
Assessed patching overlap, cytoplasmic recruitment of the src-like tyrosine kinase Fyn, and the effects of cholesterol depletion on domain segregation.
Cross-linked raft markers co-localized extensively and accumulated cytoplasmic Fyn kinase, whereas raft patches segregated sharply from non-raft transferrin receptor patches.
Cholesterol depletion abrogated the spatial segregation between raft and non-raft components, demonstrating that domain separation relies on lipid phase immiscibility.

Cite This Study

Harder et al. (1998) studied this question.

synapsesocial.com/papers/6a6f1899abc331a858078947 https://doi.org/10.1083/jcb.141.4.929

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