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Tal, a Tsg101-specific E3 ubiquitin ligase, regulates receptor endocytosis and retrovirus budding

Article Abstract:

The identification of Tal, a novel RING finger E3 ubiquitin ligase that physically associates with, and selectively ubiquitylates, Tsg101 both in vitro and in living cells is analyzed. The results revealed that by studying endocytosis of the epidermal growth factor receptor and egress of the human immunodeficiency virus, it is concluded that Tal regulates a Tsg101-associated complex is responsible for the sorting of cargo into cytoplasm-containing vesicles that bud at the mutivesicular body and at the plasma membrane.

Author: Reiss, Yuval, Amit, Ido, Marmor, Mina D., Yaara Zwang, Katz, Menachem, Yakir, Liat, Shtiegman, Keren, Citri, Ami, Alroy, Iris, Tuvia,Shmuel, Roubini, Eli, Wides, Ron, Cohen, Maya, Bacharach, Eran, Yarden, Yosef, Schubert, Ullrich
Publisher: Cold Spring Harbor Laboratory Press
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 2004
Cell membranes, Genetic research

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c-Cbl/Sli-1 regulates endocytic sorting and ubiquination of the epidermal growth factor receptor

Article Abstract:

The fate and signaling capability of growth factor receptors may be controlled by an endosomal sorting mechanism. Transient mobilization of a small amount of c-Cbl into endosomes that contain the EGF receptor ErbB-1 mediates the degradation of internalized ErbB-1 induced by ligands. ErbB-3 is differentiated by its inability to recruit c-Cbl.

Author: Yarden, Yosef, Geiger, Benjamin, Levkowitz, Gil, Waterman, Hadassa, Zamir, Eli, Kam, Zvi, Oved, Shlomo, Langdon, Wallace Y., Berguinot, Laura
Publisher: Cold Spring Harbor Laboratory Press
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 1998
Physiological aspects, Epidermal growth factor, Epidermal growth factors

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Selective assembly of a HIV-1 Vif-Cul5-ElonginB-Elongin-C E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines

Article Abstract:

A novel SOCS box in HIV-1 that mediates its interaction with ElonginC is characterized. It was found that selective assembly with Cul5 versus Cul2 E3 requires protein interfaces besides the SOCS-box-ElonginC interaction.

Author: Yunkai Yu, Zuoxiang Xiao, Ehrlich, Elana S., Xianghui Yu, Xiao-Fang Yu
Publisher: Cold Spring Harbor Laboratory Press
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 2004
Ligases, Cysteine

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Subjects list: Research, Ubiquitin, Endocytosis
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