Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Jacob A. Culver"'
Publikováno v:
Cell Reports, Vol 42, Iss 1, Pp 111921- (2023)
Summary: Tail-anchored (TA) proteins contain a single C-terminal transmembrane domain (TMD) that is captured by the cytosolic Get3 in yeast (TRC40 in humans). Get3 delivers TA proteins to the Get1/2 complex for insertion into the endoplasmic reticulu
Externí odkaz:
https://doaj.org/article/3140225396d546c5a27daedc9d467434
Autor:
Jacob A. Culver, Malaiyalam Mariappan
Publikováno v:
The Journal of Cell Biology
Culver and Mariappan show newly synthesized tail-anchored (TA) proteins are polyubiquitinated and yet are targeted properly, deubiquitinated, and inserted into the ER. The ER-localized deubiquitinases USP20/33 remove TA ubiquitin modifications. Witho
Autor:
Malaiyalam Mariappan, Jacob A. Culver
Publikováno v:
eLife
Membrane proteins with multiple transmembrane domains play critical roles in cell physiology, but little is known about the machinery coordinating their biogenesis at the endoplasmic reticulum. Here we describe a ~ 360 kDa ribosome-associated complex
Publikováno v:
Bioessays
Molecular chaperones in cells constantly monitor and bind to exposed hydrophobicity in newly synthesized proteins and assist them in folding or targeting to cellular membranes for insertion. However, proteins can be misfolded or mistargeted, which of
Publikováno v:
Biophysical Journal. 110(3)
Understanding the mechanism by which tau binds to and promotes microtubule (MT) assembly as part of its native function may also provide insight into its loss of function that occurs in neurodegenerative disease. Both mechanistic and structural studi
Publikováno v:
Biophysical Journal. 108:509a
Tau is a microtubule-associated protein which functions to maintain microtubule stability as well as promote microtubule polymerization in the axons of neurons. Its self-association and deposition as neurofibrillary tangles is also one of the primary