Cell-surface transglutaminase undergoes internalization and lysosomal degradation: an essential role for LRP1.

Cell-surface transglutaminase undergoes internalization and lysosomal degradation: an essential role for LRP1. Research Abstract Details 

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Cell-surface transglutaminase undergoes internalization and lysosomal degradation: an essential role for LRP1. Abstract Text:

Evgeny A Zemskov,Irina Mikhailenko,Dudley K Strickland,Alexey M Belkin,

Tissue transglutaminase functions as a protein crosslinking enzyme and an integrin-binding adhesion co-receptor for fibronectin on the cell surface. These activities of transglutaminase and the involvement of this protein in cell-matrix adhesion, integrin-mediated signaling, cell migration and matrix organization suggest a precise and efficient control of its cell-surface expression. We report a novel mechanism of regulation of surface transglutaminase through internalization and subsequent lysosomal degradation. Constitutive endocytosis of cell-surface transglutaminase depends on plasma membrane cholesterol and the activity of dynamin-2, and involves both clathrin-coated pits and lipid rafts or caveolae. Furthermore, the key matrix ligands of transglutaminase, fibronectin and platelet-derived growth factor, promote its endocytosis from the cell surface. Our results also indicate that transglutaminase interacts in vitro and on the cell surface with the major endocytic receptor, low-density lipoprotein receptor-related protein 1, and demonstrate the requirement for this receptor in the endocytosis of transglutaminase. Finally, a deficiency of this endocytic receptor or blockade of endo-lysosomal function upregulate transglutaminase expression on the cell surface, leading to increased cell adhesion and matrix crosslinking. These findings characterize a previously unknown pathway of transglutaminase internalization and degradation that might be crucial for regulation of its adhesive and signaling functions on the cell surface and reveal a novel functional link between cell-matrix adhesion and endocytosis.

Cell-surface transglutaminase undergoes internalization and lysosomal degradation: an essential role for LRP1. Publishing Authors By Initials

EA Zemskov,I Mikhailenko,DK Strickland,AM Belkin,

For similar proteins: neoplasm proteins: tumor suppressor proteins research abstracts see: proteins: neoplasm proteins: tumor suppressor proteins research

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Cell-surface transglutaminase undergoes internalization and lysosomal degradation: an essential role for LRP1. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Journal of cell science

VOLUME: 120

Page Numbers: 3188-99

Journal Abbreviation: J. Cell. Sci.

ISSN: 0021-9533

DAY: 21

MONTH: 08

YEAR: 2007

Cell-surface transglutaminase undergoes internalization and lysosomal degradation: an essential role for LRP1. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 52457

Cell-surface transglutaminase undergoes internalization and lysosomal degradation: an essential role for LRP1. Keywords Mesh Terms:

KEYWORDS: Tumor Suppressor Proteins

MESH TERMS: metabolism

Chemical & Substance for Abstract: Cell-surface transglutaminase undergoes internalization and lysosomal degradation: an essential role for LRP1. Information

Substance Name: Dynamin II

Registry Number: EC 3.6.1.50

Grant and Affiliation Information for Cell-surface transglutaminase undergoes internalization and lysosomal degradation: an essential role for LRP1.

AFFILIATION: Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.

Country: England

AGENCY: United States NHLBI

GRANT: HL50784

ACRONYM: HL

MEDLINETA: J Cell Sci

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