Rab GTPases mature the LC3-associated midbody phagosome

نویسندگان

  • Gholamreza Fazeli
  • Ann Marie Wehman
چکیده

ARTICLE HISTORY Received 12 December 2016 Revised 16 February 2017 Accepted 16 February 2017 ABSTRACT Post-mitotic midbody remnants have recently been added to the list of structures degraded via LC3associated phagocytosis (LAP). LAP involves proteins of the autophagy pathway to degrade phagosomal contents, mingling 2 pathways that were thought to be distinct. To better characterize how similar LAP is to classical phagocytosis, we asked whether the midbody LAPosome (LC3associated phagosome) matures using Rab GTPases in C. elegans embryos. We found that RAB-5 and RAB-7 appear transiently on midbody LAPosomes and that RAB-7 is required for midbody degradation, suggesting that RAB-5 and RAB-7 direct LAPosome maturation similar to classical phagosomes. Further, we observed that the Rab2 homolog UNC-108 and the major proton pump, the V-type ATPase, are required for acidification of the midbody LAPosome, demonstrating that phagosomes and LAPosomes acidify via a common pathway. Together, these data reveal that Rab GTPases play similar roles during LAPosome maturation and phagosome maturation.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

C. elegans midbodies are released, phagocytosed and undergo LC3-dependent degradation independent of macroautophagy

In animals, the midbody coordinates the end of cytokinesis when daughter cells separate through abscission. The midbody was thought to be sequestered by macroautophagy, but recent evidence suggests that midbodies are primarily released and phagocytosed. It was unknown, however, whether autophagy proteins play a role in midbody phagosome degradation. Using a protein degradation assay, we show th...

متن کامل

Functional role(s) of phagosomal Rab GTPases

Rab GTPases are at the central node of the machinery that regulates trafficking of organelles, including phagosomes. Thanks to the unique combination of high quality phagosome purification with highly sensitive proteomic studies, the network of Rab proteins that are dynamically associated with phagosomes during the process of maturation of this organelle is relatively well known. Whereas the ph...

متن کامل

A network of Rab GTPases controls phagosome maturation and is modulated by Salmonella enterica serovar Typhimurium

Members of the Rab guanosine triphosphatase (GTPase) family are key regulators of membrane traffic. Here we examined the association of 48 Rabs with model phagosomes containing a non-invasive mutant of Salmonella enterica serovar Typhimurium (S. Typhimurium). This mutant traffics to lysosomes and allowed us to determine which Rabs localize to a maturing phagosome. In total, 18 Rabs associated w...

متن کامل

Sequential action of Caenorhabditis elegans Rab GTPases regulates phagolysosome formation during apoptotic cell degradation.

Phagocytosis of apoptotic cells requires recognition of cell corpses followed by internalization and enclosure within plasma membrane-derived phagosomes. Phagosomes undergo maturation to generate phagolysosomes in which cell corpses are degraded; however, regulation of the maturation process is poorly understood. Here, we identified Rab GTPase 14, which regulates apoptotic cell degradation in C...

متن کامل

Staphylococcus aureus Alpha-Toxin Induces the Formation of Dynamic Tubules Labeled with LC3 within Host Cells in a Rab7 and Rab1b-Dependent Manner

Staphylococcus aureus is a pathogen that causes severe infectious diseases that eventually lead to septic and toxic shock. S. aureus infection is characterized by the production of virulence factors, including enzymes and toxins. After internalization S. aureus resides in a phagosome labeled with Rab7 protein. Here, we show that S. aureus generates tubular structures marked with the small GTPas...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره 10  شماره 

صفحات  -

تاریخ انتشار 2017