000			01599nam a2200229Ia 4500
003			MX-MdCICY
005			20250625162452.0
040			_cCICY
090			_aB-20622
245	1	0	_aThe midnolin-proteasome pathway catches proteins for ubiquitination-independent degradation
490	0		_vScience, 381(6660), p.eadh5021, 2023
520	3		_aCells use ubiquitin to mark proteins for proteasomal degradation. Although the proteasome also eliminates proteins that are not ubiquitinated, how this occurs mechanistically is unclear. Here, we found that midnolin promoted the destruction of many nuclear proteins, including transcription factors encoded by the immediate-early genes. Diverse stimuli induced midnolin, and its overexpression was sufficient to cause the degradation of its targets by a mechanism that did not require ubiquitination. Instead, midnolin associated with the proteasome via an ? helix, used its Catch domain to bind a region within substrates that can form a ? strand, and used a ubiquitin-like domain to promote substrate destruction. Thus, midnolin contains three regions that function in concert to target a large set of nuclear proteins to the proteasome for degradation.
700	1	2	_aGu, X.
700	1	2	_aNardone, C.
700	1	2	_aKamitaki, N.
700	1	2	_aMao, A.
700	1	2	_aElledge, S. J.
700	1	2	_aGreenberg, M. E.
856	4	0	_uhttps://drive.google.com/file/d/1xKet5r2rKS71fKnn_E2zfhjW_QS4ztFS/view?usp=drivesdk _zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
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