Investigation into the mechanism regulating MRP localization.

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Investigation into the mechanism regulating MRP localization. Abstract Text:

Iman van den Bout,Jacco van Rheenen,Annelies A van Angelen,Johan de Rooij,Kevin Wilhelmsen,Kees Jalink,Nullin Divecha,Arnoud Sonnenberg,Iman van den Bout,Jacco van Rheenen,Annelies A van Angelen,Johan de Rooij,Kevin Wilhelmsen,Kees Jalink,Nullin Divecha,Arnoud Sonnenberg,

The major PKC substrates MARCKS and MacMARCKS (MRP) are membrane-binding proteins implicated in cell spreading, integrin activation and exocytosis. According to the myristoyl-electrostatic switch model the co-operation between the myristoyl moiety and the positively charged effector domain (ED) is an essential mechanism by which proteins bind to membranes. Loss of the electrostatic interaction between the ED and phospholipids, such as Ptdins(4,5)P2, results in the translocation of such proteins to the cytoplasm. While this model has been extensively tested for the binding of MARCKS far less is known about the mechanisms regulating MRP localization. We demonstrate that after phosphorylation, MRP is relocated to the intracellular membranes of late endosomes and lysosomes. MRP binds to all membranes via its myristoyl moiety, but for its localization at the plasma membrane the ED is also required. Although the ED of MRP can bind to Ptdins(4,5)P2 in vitro, this binding is not essential for its retention at or targeting to the plasma membrane. We conclude that the co-operation between the myristoyl moiety and the ED is not required for the binding to membranes in general but that it is essential for the targeting of MRP to the plasma membrane in a Ptdins(4,5)P2-independent manner.

Investigation into the mechanism regulating MRP localization. Publishing Authors By Initials

I van den Bout,J van Rheenen,AA van Angelen,J de Rooij,K Wilhelmsen,K Jalink,N Divecha,A Sonnenberg,I van den Bout,J van Rheenen,AA van Angelen,J de Rooij,K Wilhelmsen,K Jalink,N Divecha,A Sonnenberg,

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Investigation into the mechanism regulating MRP localization. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Experimental cell research

VOLUME: 314

Page Numbers: 330-41

Journal Abbreviation: Exp. Cell Res.

ISSN: 0014-4827

DAY: 29

MONTH: 08

YEAR: 2007

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LANGUAGE: eng

NlmUniqueID: 373226

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AFFILIATION: Division of Cell Biology, Netherlands Cancer Institute, 121 Plesmanlaan, 1066 CX Amsterdam, The Netherlands.

Country: United States

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MEDLINETA: Exp Cell Res

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