Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Sarah B Nyenhuis"'
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-15 (2024)
Abstract The translocation and assembly module (TAM) has been proposed to play a crucial role in the assembly of a small subset of outer membrane proteins (OMPs) in Proteobacteria based on experiments conducted in vivo using tamA and tamB mutant stra
Externí odkaz:
https://doaj.org/article/f16dae8ac5b74630aff73f288299dd2a
Autor:
Ángel Pérez-Lara, Anusa Thapa, Sarah B Nyenhuis, David A Nyenhuis, Partho Halder, Michael Tietzel, Kai Tittmann, David S Cafiso, Reinhard Jahn
Publikováno v:
eLife, Vol 5 (2016)
The Ca2+-sensor synaptotagmin-1 that triggers neuronal exocytosis binds to negatively charged membrane lipids (mainly phosphatidylserine (PtdSer) and phosphoinositides (PtdIns)) but the molecular details of this process are not fully understood. Usin
Externí odkaz:
https://doaj.org/article/c02207f7628d429d958a8be352713cec
Autor:
Sarah B. Nyenhuis, Nakul Karandikar, Volker Kiessling, Alex J. B. Kreutzberger, Anusa Thapa, Binyong Liang, Lukas K. Tamm, David S. Cafiso
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
Synaptotagmin 1 (Syt1) is the calcium sensor for fast synchronous neurotransmitter release but the mechanism by which it functions is still under debate. Here, the authors combine EPR measurements and functional studies and observe that different fac
Externí odkaz:
https://doaj.org/article/81777fc5abd14f21a6ee0ae5308e9f0f
Autor:
Sarah B. Nyenhuis, Xufeng S. Wu, Abigail Stanton, Marie-Paule Strub, Yang-In Yim, Bertram J. Canagarajah, Jenny E. Hinshaw
Publikováno v:
Biophysical Journal. 122:303a
Autor:
Samantha Bryce, Sarah B. Nyenhuis, Daniel Crosby, Jenny E. Hinshaw, Melissa R. Mikolaj, Tina H. Lee
Publikováno v:
Journal of Cell Biology. 221
ER network formation depends on membrane fusion by the atlastin (ATL) GTPase. In humans, three paralogs are differentially expressed with divergent N- and C-terminal extensions, but their respective roles remain unknown. This is partly because, unlik
Publikováno v:
Biophys J
Synaptotagmin 1 acts as the Ca2+-sensor for synchronous neurotransmitter release; however, the mechanism by which it functions is not understood and is presently a topic of considerable interest. Here we describe measurements on full-length membrane
Autor:
Nakul Karandikar, Alex J. B. Kreutzberger, Lukas K. Tamm, Binyong Liang, Anusa Thapa, David S. Cafiso, Volker Kiessling, Sarah B. Nyenhuis
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
Nature Communications
Nature Communications
Synaptotagmin 1 is a vesicle-anchored membrane protein that functions as the Ca2+ sensor for synchronous neurotransmitter release. In this work, an arginine containing region in the second C2 domain of synaptotagmin 1 (C2B) is shown to control the ex
Publikováno v:
Biophys J
Synaptotagmin 1 (Syt1) is an integral membrane protein whose phospholipid-binding tandem C2 domains, C2A and C2B, act as Ca(2+) sensors of neurotransmitter release. Our objective was to understand the role of individual metal-ion binding sites of the
Autor:
Sarah B. Nyenhuis, David S. Cafiso
Publikováno v:
Protein Science. 27:1008-1012
Synaptotagmin-1 (Syt1) functions as the Ca2+ sensor in neuronal exocytosis, and it is routinely incorporated into lipid bilayers along with other components of the fusion machinery in order to reconstruct the in vivo fusion process. Here, we demonstr
Autor:
Alexander B. Taylor, Bin Her, Atul K. Srivastava, Tatyana I. Igumenova, Sachin Katti, P. John Hart, David S. Cafiso, Sarah B. Nyenhuis
Publikováno v:
Biochemistry. 56:3283-3295
C2 domains are independently folded modules that often target their host proteins to anionic membranes in a Ca2+-dependent manner. In these cases, membrane association is triggered by Ca2+ binding to the negatively charged loop region of the C2 domai