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Unconventional Secretion of Tissue Transglutaminase Involves Phospholipid-Dependent Delivery into Recycling Endosomes

  1. Author:
    Zemskov, E. A.
    Mikhailenko, I.
    Hsia, R. C.
    Zaritskaya, L.
    Belkin, A. M.

  2. Author Address

    [Zemskov, EA; Belkin, AM] Univ Maryland, Sch Med, Dept Biochem & Mol Biol, Baltimore, MD 21201 USA [Zemskov, EA; Mikhailenko, I; Belkin, AM] Univ Maryland, Sch Med, Ctr Vasc & Inflammatory Dis, Baltimore, MD 21201 USA [Mikhailenko, I] Univ Maryland, Sch Med, Dept Physiol, Baltimore, MD 21201 USA [Belkin, AM] Univ Maryland, Sch Med, Marlene & Stewart Greenebaum Canc Ctr, Baltimore, MD 21201 USA [Belkin, AM] Univ Maryland, Sch Med, Ctr Stem Cell Biol & Regenerat Med, Baltimore, MD 21201 USA [Hsia, RC] Univ Maryland, Sch Dent, Core Imaging Facil, Baltimore, MD 21201 USA [Zaritskaya, L] Sci Applicat Int Corp, Appl & Dev Res Support Program, Frederick, MD USA;Zemskov, EA (reprint author), Univ Maryland, Sch Med, Dept Biochem & Mol Biol, Baltimore, MD 21201 USA;abelkin@som.umaryland.edu
    1. Year: 2011
    2. Date: Apr
  2. Journal: Plos One
    1. 6
    2. 4
    3. Pages: 14
  4. Type of Article: Article
  5. Article Number: e19414
  6. ISSN: 1932-6203
  1. Abstract:

    Although endosomal compartments have been suggested to play a role in unconventional protein secretion, there is scarce experimental evidence for such involvement. Here we report that recycling endosomes are essential for externalization of cytoplasmic secretory protein tissue transglutaminase (tTG). The de novo synthesized cytoplasmic tTG does not follow the classical ER/Golgi-dependent secretion pathway, but is targeted to perinuclear recycling endosomes, and is delivered inside these vesicles prior to externalization. On its route to the cell surface tTG interacts with internalized beta 1 integrins inside the recycling endosomes and is secreted as a complex with recycled beta 1 integrins. Inactivation of recycling endosomes, blocking endosome fusion with the plasma membrane, or downregulation of Rab11 GTPase that controls outbound trafficking of perinuclear recycling endosomes, all abrogate tTG secretion. The initial recruitment of cytoplasmic tTG to recycling endosomes and subsequent externalization depend on its binding to phosphoinositides on endosomal membranes. These findings begin to unravel the unconventional mechanism of tTG secretion which utilizes the long loop of endosomal recycling pathway and indicate involvement of endosomal trafficking in non-classical protein secretion.

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External Sources

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  2. DOI: 10.1371/journal.pone.0019414
  3. View record in Web of Science®
  4. WOS: 000290019400058

Library Notes

  1. Fiscal Year: FY2010-2011
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