FIGURE

Fig. 5

ID

ZDB-FIG-100302-55

Publication

Seo et al., 2010 - BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and mediate BBSome assembly

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Fig. 5

Many disease-causing missense mutations found in BBS6, BBS10, and BBS12 disrupt interactions among these proteins. (A) Interactions of BBS6 missense mutants with BBS12. HEK293T cells were transfected with Myc-BBS12 together with HA-BBS6 variants and lysates were subject to coimmunoprecipitation (IP) and immunoblotting (IB). Numbers at bottom represent ratio of coprecipitated proteins compared with wild-type protein after normalization with input. (B) Interactions of BBS10 missense mutants with BBS12. (C) Interactions of BBS12 missense mutants with BBS6. (D) Model for BBS/CCT complex function. BBS/CCT complex initially binds to BBS7 and potentially to BBS2, and mediates their association with other BBSome subunits (BBS1,4,5,8,9) to assemble BBSome. When chaperonin-like BBS genes are inactivated, at least two BBSome subunits (BBS2 and BBS7) are degraded, and the remaining BBSome subunits exist in monomeric form or aggregates with unidentified proteins.

Expression Data

Expression Detail

Antibody Labeling

Phenotype Data

Phenotype Detail

Acknowledgments

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Full text @ Proc. Natl. Acad. Sci. USA