Tubulation of class II MHC compartments is microtubule dependent and involves multiple endolysosomal membrane proteins in primary dendritic cells.

Tubulation of class II MHC compartments is microtubule dependent and involves multiple endolysosomal membrane proteins in primary dendritic cells. Research Abstract Details 

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Tubulation of class II MHC compartments is microtubule dependent and involves multiple endolysosomal membrane proteins in primary dendritic cells. Abstract Text:

Jatin M Vyas,You-Me Kim,Katerina Artavanis-Tsakonas,J Christopher Love,Annemarthe G Van der Veen,Hidde L Ploegh,

Immature dendritic cells (DCs) capture exogenous Ags in the periphery for eventual processing in endolysosomes. Upon maturation by TLR agonists, DCs deliver peptide-loaded class II MHC molecules from these compartments to the cell surface via long tubular structures (endolysosomal tubules). The nature and rules that govern the movement of these DC compartments are unknown. In this study, we demonstrate that the tubules contain multiple proteins including the class II MHC molecules and LAMP1, a lysosomal resident protein, as well as CD63 and CD82, members of the tetraspanin family. Endolysosomal tubules can be stained with acidotropic dyes, indicating that they are extensions of lysosomes. However, the proper trafficking of class II MHC molecules themselves is not necessary for endolysosomal tubule formation. DCs lacking MyD88 can also form endolysosomal tubules, demonstrating that MyD88-dependent TLR activation is not necessary for the formation of this compartment. Endolysosomal tubules in DCs exhibit dynamic and saltatory movement, including bidirectional travel. Measured velocities are consistent with motor-based movement along microtubules. Indeed, nocodazole causes the collapse of endolysosomal tubules. In addition to its association with microtubules, endolysosomal tubules follow the plus ends of microtubules as visualized in primary DCs expressing end binding protein 1 (EB1)-enhanced GFP.

Tubulation of class II MHC compartments is microtubule dependent and involves multiple endolysosomal membrane proteins in primary dendritic cells. Publishing Authors By Initials

JM Vyas,YM Kim,K Artavanis-Tsakonas,JC Love,AG Van der Veen,HL Ploegh,

For similar biochemical phenomena, metabolism, and nutrition: metabolism: biological transport: protein transport research abstracts see: biochemical phenomena, metabolism, and nutrition: metabolism: biological transport: protein transport research

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Tubulation of class II MHC compartments is microtubule dependent and involves multiple endolysosomal membrane proteins in primary dendritic cells. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of immunology (Baltimore, Md. : 1950)

VOLUME: 178

Page Numbers: 7199-210

Journal Abbreviation: J. Immunol.

ISSN: 0022-1767

DAY: 1

MONTH: Jun

YEAR: 2007

Tubulation of class II MHC compartments is microtubule dependent and involves multiple endolysosomal membrane proteins in primary dendritic cells. Information

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LANGUAGE: eng

NlmUniqueID: 2985117

Tubulation of class II MHC compartments is microtubule dependent and involves multiple endolysosomal membrane proteins in primary dendritic cells. Keywords Mesh Terms:

KEYWORDS: Protein Transport

MESH TERMS: immunology

Chemical & Substance for Abstract: Tubulation of class II MHC compartments is microtubule dependent and involves multiple endolysosomal membrane proteins in primary dendritic cells. Information

Substance Name: Nocodazole

Registry Number: 31430-18-9

Grant and Affiliation Information for Tubulation of class II MHC compartments is microtubule dependent and involves multiple endolysosomal membrane proteins in primary dendritic cells.

AFFILIATION: Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA.

Country: United States

AGENCY: United States NIAID

GRANT: 5R01AI034893-13

ACRONYM: AI

MEDLINETA: J Immunol

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