Annexin A2 promotes phagophore assembly by enhancing Atg16L+ vesicle biogenesis and homotypic fusion

Kateryna Morozova, Sunandini Sidhar, Valerio Zolla, Cristina C. Clement, Brian Scharf, Zoe Verzani, Antonio Diaz, Jorge N. Larocca, Katherine A. Hajjar, Ana Maria Cuervo and Laura Santambrogio ()
Additional contact information
Kateryna Morozova: Albert Einstein College of Medicine
Sunandini Sidhar: Albert Einstein College of Medicine
Valerio Zolla: Albert Einstein College of Medicine
Cristina C. Clement: Albert Einstein College of Medicine
Brian Scharf: Albert Einstein College of Medicine
Zoe Verzani: Albert Einstein College of Medicine
Antonio Diaz: Albert Einstein College of Medicine
Jorge N. Larocca: Albert Einstein College of Medicine
Katherine A. Hajjar: Weill Cornell Medical College
Ana Maria Cuervo: Albert Einstein College of Medicine
Laura Santambrogio: Albert Einstein College of Medicine

Nature Communications, 2015, vol. 6, issue 1, 1-12

Abstract: Abstract Plasma membrane budding of Atg-16L-positive vesicles represents a very early event in the generation of the phagophore and in the process of macroautophagy. Here we show that the membrane curvature-inducing protein annexin A2 contributes to the formation of these vesicles and their fusion to form phagophores. Ultrastructural, proteomic and FACS analyses of Atg16L-positive vesicles reveal that 30% of Atg16L-positive vesicles are also annexin A2-positive. Lipidomic analysis of annexin A2-deficient mouse cells indicates that this protein plays a role in recruiting phosphatidylserine and phosphatidylinositides to Atg16L-positive vesicles. Absence of annexin A2 reduces both vesicle formation and homotypic Atg16L vesicle fusion. Ultimately, a reduction in LC3 flux and dampening of macroautophagy are observed in dendritic cells from Anxa2−/− mice. Together, our analyses highlight the importance of annexin A2 in vesiculation of a population of Atg16L-positive structures from the plasma membrane, and in their homotypic fusion to form phagophore structures.

Date: 2015
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/ncomms6856 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms6856

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms6856

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().