The C-terminal transmembrane domain of human phospholipid scramblase 1 is essential for the protein flip-flop activity and Ca²⁺-binding. (Q43672114)

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3 March 2020

title

The C-terminal transmembrane domain of human phospholipid scramblase 1 is essential for the protein flip-flop activity and Ca²⁺-binding (English)

1 reference

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3 March 2020

main subject

transmembrane protein

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author

Ana Rosa Viguera

5

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3 March 2020

Diego M.A. Guérin

6

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3 March 2020

Hugo L Monaco

8

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3 March 2020

author name string

Lissete Sánchez-Magraner

1

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3 March 2020

Itziar M D Posada

2

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3 March 2020

Nagore Andraka

3

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3 March 2020

F Xabier Contreras

4

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3 March 2020

José L R Arrondo

7

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3 March 2020

Félix M Goñi

9

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3 March 2020

publication date

17 December 2013

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3 March 2020

number of pages

11

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Journal of Membrane Biology

inferred from page(s)

published in

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3 March 2020

volume

247

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3 March 2020

issue

2

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3 March 2020

page(s)

155-165

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Phospholipid scramblase 1 modulates a selected set of IgE receptor-mediated mast cell responses through LAT-dependent pathway

3 March 2020

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The single C-terminal helix of human phospholipid scramblase 1 is required for membrane insertion and scrambling activity.

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Interaction of the phospholipid scramblase 1 with HIV-1 Tat results in the repression of Tat-dependent transcription.

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The phospholipid scramblases 1 and 4 are cellular receptors for the secretory leukocyte protease inhibitor and interact with CD4 at the plasma membrane

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Plasma membrane phospholipid scramblase 1 is enriched in lipid rafts and interacts with the epidermal growth factor receptor

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Calcium-dependent phospholipid scrambling by TMEM16F

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Identification of three new members of the phospholipid scramblase gene family

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Palmitoylation of phospholipid scramblase 1 controls its distribution between nucleus and plasma membrane

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Interaction with a membrane surface triggers a reversible conformational change in Bax normally associated with induction of apoptosis

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Palmitoylation of phospholipid scramblase is required for normal function in promoting Ca2+-activated transbilayer movement of membrane phospholipids

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