The CAP-Gly Domain of CYLD Associates with the Proline-Rich Sequence in NEMO/IKKγ

Saito, Kohei; Kigawa, T.; Koshiba, S.; Sato, Ken-iti; Matsuo, Yo; Sakamoto, Ayako; Takagi, Tetsuo; Shirouzu, Mikako; Yabuki, Takashi; Nunokawa, Emi; Seki, Eiko; Matsuda, Takayoshi; Aoki, Masaaki; Miyata, Yukako; Hirakawa, Naoya; Inoue, Makoto; Terada, Takaho; Nagase, Takahiro; Kikuno, Reiko; Nakayama, Manabu; Ohara, Osamu; Tanaka, Akiko; Yokoyama, Shigeyuki

doi:10.1016/j.str.2004.07.012

Cited by 97 publications

(83 citation statements)

References 54 publications

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“…Our studies revealed that the CAP-Gly domain may also function as a no-tubulin-binding module. Consistent with this notion, a similar finding was reported for the Cyld protein, a regulator of p53 (33).…”

Section: Discussionsupporting

confidence: 86%

ClipR-59 Interacts with Akt and Regulates Akt Cellular Compartmentalization

Ding

2009

Molecular and Cellular Biology

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Akt is activated on the plasma membrane and its substrates are distributed throughout various cellular compartments. To phosphorylate its substrates, Akt needs to be recruited to specific intracellular compartments. Thus, regulation of Akt cellular compartmentalization constitutes an important mechanism to specify Akt signaling. Here, we report the identification of ClipR-59 as an Akt interaction protein. We show that the interaction of ClipR-59 with Akt is mediated by the CAP-Gly domain of ClipR-59 and kinase domain of Akt and is regulated by Akt phosphorylation. We demonstrate that ClipR-59 regulates the Akt membrane association through its interaction with Akt and membrane localization and, by modulating Akt cellular compartmentalization, differentially modulates phosphorylation of Akt substrates in adipocytes. Finally, we provide evidence that one of the Akt substrates whose phosphorylation is upregulated by ClipR-59 is AS160, a negative regulator of adipocyte glucose transport. Accordingly, ectopic expression of ClipR-59 enhances, whereas knockdown of ClipR-59 suppresses, adipocyte glucose transport. We suggest that ClipR-59 functions as a scaffold protein that interacts with phospho-Akt and recruits active Akt on the membrane and may play an important role in adipocyte glucose transport.

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Section: Discussionsupporting

confidence: 86%

ClipR-59 Interacts with Akt and Regulates Akt Cellular Compartmentalization

Ding

2009

Molecular and Cellular Biology

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“…63 Both TRAF6 Lys124 and IKK␥ Lys399 are within close proximity to at least one of the USP7 consensus binding motifs, potentially enabling USP7 to dock in close proximity to polyubiquitinated lysine residues. Further supporting this hypothesis, the 2 P/AXXS USP7-binding motifs within IKK␥ are located 4 residues from the binding site (aa's 388-393) 64 of CYLD.…”

Section: Discussionmentioning

confidence: 70%

HSV ICP0 recruits USP7 to modulate TLR-mediated innate response

Daubeuf

Singh

Tan

et al. 2009

Blood

127

128

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“…The cytoskeleton-associated protein glycinerich (CAP-Gly) domain is a small globular module that contains a unique conserved hydrophobic cavity and several characteristic glycine residues (Li et al, 2002;Saito et al, 2004). CAP-Gly domains use their hydrophobic cavity to confer interactions with microtubules and EB proteins by specifically recognizing C-terminal EEY/F sequence motifs (Honnappa et al, 2006;Mishima et al, 2007;Weisbrich et al, 2007).…”

Section: D Lattice Diffusion (Mcak Xmap215)mentioning

confidence: 99%