F-Box Proteins Are Receptors that Recruit Phosphorylated Substrates to the SCF Ubiquitin-Ligase Complex Export

@article{citeulike:2799880, abstract = {We have reconstituted the ubiquitination pathway for the Cdk inhibitor Sic1 using recombinant proteins. Skp1, Cdc53, and the F-box protein Cdc4 form a complex, SCFCdc4, which functions as a Sic1 ubiquitin-ligase (E3) in combination with the ubiquitin conjugating enzyme (E2) Cdc34 and E1. Cdc4 assembled with Skp1 functions as the receptor that selectively binds phosphorylated Sic1. Grr1, an F-box protein involved in Cln destruction, forms complexes with Skp1 and Cdc53 and binds phosphorylated Cln1 and Cln2, but not Sic1. Because the constituents of the SCF complex are members of protein families, SCFCdc4 is likely to serve as the prototype for a large class of E3s formed by combinatorial interactions of related family members. SCF complexes couple protein kinase signaling pathways to the control of protein abundance.}, author = {Skowyra, Dorota and Craig, Karen L. and Tyers, Mike and Elledge, Stephen J. and Harper, Wade J.}, citeulike-article-id = {2799880}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/S0092-8674(00)80403-1}, citeulike-linkout-1 = {http://www.sciencedirect.com/science/article/B6WSN-418PXFJ-8/1/7adc0674eefb3d52dc5c5bb33574a56e}, day = {17}, doi = {10.1016/S0092-8674(00)80403-1}, journal = {Cell}, keywords = {arrest, cdc4, cell, cycle, f-box, phase, regulation}, month = {October}, number = {2}, pages = {209--219}, posted-at = {2008-05-14 20:55:53}, priority = {2}, title = {F-Box Proteins Are Receptors that Recruit Phosphorylated Substrates to the SCF Ubiquitin-Ligase Complex}, url = {http://dx.doi.org/10.1016/S0092-8674(00)80403-1}, volume = {91}, year = {1997} }

TY - JOUR ID - citeulike:2799880 L3 - citeulike-article-id:2799880 N2 - We have reconstituted the ubiquitination pathway for the Cdk inhibitor Sic1 using recombinant proteins. Skp1, Cdc53, and the F-box protein Cdc4 form a complex, SCFCdc4, which functions as a Sic1 ubiquitin-ligase (E3) in combination with the ubiquitin conjugating enzyme (E2) Cdc34 and E1. Cdc4 assembled with Skp1 functions as the receptor that selectively binds phosphorylated Sic1. Grr1, an F-box protein involved in Cln destruction, forms complexes with Skp1 and Cdc53 and binds phosphorylated Cln1 and Cln2, but not Sic1. Because the constituents of the SCF complex are members of protein families, SCFCdc4 is likely to serve as the prototype for a large class of E3s formed by combinatorial interactions of related family members. SCF complexes couple protein kinase signaling pathways to the control of protein abundance. IS - 2 JF - Cell EP - 219 TI - F-Box Proteins Are Receptors that Recruit Phosphorylated Substrates to the SCF Ubiquitin-Ligase Complex VL - 91 SP - 209 KW - arrest KW - cdc4 KW - cell KW - cycle KW - f-box KW - phase KW - regulation AU - Skowyra, Dorota AU - Craig, Karen AU - Tyers, Mike AU - Elledge, Stephen AU - Harper, Wade PY - 1997/10/17/ UR - http://dx.doi.org/10.1016/S0092-8674(00)80403-1 ER -