Multivalent endosome targeting by homodimeric EEA1 (Q24291994)

protein homodimerization activity

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

author name string

J J Dumas

1

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E Merithew

2

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E Sudharshan

3

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D Rajamani

4

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S Hayes

5

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D Lawe

6

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S Corvera

7

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D G Lambright

Phosphatidylinositol(3)-phosphate signaling mediated by specific binding to RING FYVE domains

8

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language of work or name

English

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publication date

November 2001

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published in

Molecular Cell

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volume

8

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page(s)

947-58

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issue

5

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cites work

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7 January 2021

The endosome fusion regulator early-endosomal autoantigen 1 (EEA1) is a dimer

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The Rab5 effector EEA1 is a core component of endosome docking

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Direct targets of phosphoinositide 3-kinase products in membrane traffic and signal transduction

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Phosphoinositides in membrane traffic

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Using structure to define the function of phosphoinositide 3-kinase family members

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FYVE fingers bind PtdIns(3)P

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Interaction of the EEA1 FYVE finger with phosphatidylinositol 3-phosphate and early endosomes. Role of conserved residues

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Localization of phosphatidylinositol 3-phosphate in yeast and mammalian cells

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Cellular functions of phosphatidylinositol 3-phosphate and FYVE domain proteins

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Improved methods for building protein models in electron density maps and the location of errors in these models

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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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Structural mechanism of endosome docking by the FYVE domain

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Phosphatidylinositol 3-Phosphate Recognition by the FYVE Domain

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[27] Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods.

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The FYVE domain of early endosome antigen 1 is required for both phosphatidylinositol 3-phosphate and Rab5 binding. Critical role of this dual interaction for endosomal localization

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Signalling through phosphoinositide 3-kinases: the lipids take centre stage

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Signal-dependent membrane targeting by pleckstrin homology (PH) domains

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Crystal structure of the VHS and FYVE tandem domains of Hrs, a protein involved in membrane trafficking and signal transduction

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7 January 2021

Oligomeric complexes link Rab5 effectors with NSF and drive membrane fusion via interactions between EEA1 and syntaxin 13

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Raster3D: photorealistic molecular graphics

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Involvement of the endosomal autoantigen EEA1 in homotypic fusion of early endosomes.

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Regulation of endosome fusion.

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Crystal structure of a phosphatidylinositol 3-phosphate-specific membrane-targeting motif, the FYVE domain of Vps27p

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7 January 2021

Hgs (Hrs), a FYVE domain protein, is involved in Smad signaling through cooperation with SARA.

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7 January 2021

EEA1, an early endosome-associated protein. EEA1 is a conserved alpha-helical peripheral membrane protein flanked by cysteine "fingers" and contains a calmodulin-binding IQ motif

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Identification of an early endosomal protein regulated by phosphatidylinositol 3-kinase.

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A functional PtdIns(3)P-binding motif.

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The role of phosphoinositide 3-kinase lipid products in cell function

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Selective membrane recruitment of EEA1 suggests a role in directional transport of clathrin-coated vesicles to early endosomes

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7 January 2021

High-affinity binding of a FYVE domain to phosphatidylinositol 3-phosphate requires intact phospholipid but not FYVE domain oligomerization

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7 January 2021

EEA1 links PI(3)K function to Rab5 regulation of endosome fusion

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7 January 2021

The Rab5 effector EEA1 interacts directly with syntaxin-6

1 reference

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7 January 2021

Endosomal localization of the autoantigen EEA1 is mediated by a zinc-binding FYVE finger

1 reference

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7 January 2021