The Actin-depolymerizing Factor Homology and Charged/Helical Domains of Drebrin and mAbp1 Direct Membrane Binding and Localization via Distinct Interactions with Actin-Reference-Cited by-同舟云学术

The Actin-depolymerizing Factor Homology and Charged/Helical Domains of Drebrin and mAbp1 Direct Membrane Binding and Localization via Distinct Interactions with Actin

Published:2006-04 Issue:17 Volume:281 Page:11826-11833
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Xu Weidong,Stamnes Mark

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference30 articles.

1. BI-DIRECTIONAL PROTEIN TRANSPORT BETWEEN THE ER AND GOLGI

2. Regulating the actin cytoskeleton during vesicular transport

3. Cytosol-derived proteins are sufficient for Arp2/3 recruitment and ARF/coatomer-dependent actin polymerization on Golgi membranes

4. Myosin Motors and Not Actin Comets Are Mediators of the Actin-based Golgi-to-Endoplasmic Reticulum Protein Transport

5. Golgi Vesicle Proteins Are Linked to the Assembly of an Actin Complex Defined by mAbp1

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1. The multifunctional adaptor protein HIP-55 couples Smad7 to accelerate TGF-β type I receptor degradation;Acta Pharmacologica Sinica;2021-07-30

2. Drebrin controls scar formation and astrocyte reactivity upon traumatic brain injury by regulating membrane trafficking;Nature Communications;2021-03-05

3. Drebrin mediates scar formation and astrocyte reactivity during brain injury by inducing RAB8 tubular endosomes;2020-06-05

4. Drebrin Isoforms Critically Regulate NMDAR- and mGluR-Dependent LTD Induction;Frontiers in Cellular Neuroscience;2018-10-08

5. The Role of Drebrin in Cancer Cell Invasion;Advances in Experimental Medicine and Biology;2017