scholarly journals Functional characterization of the lysosomal membrane protein TMEM192 in mice

Oncotarget ◽  
2017 ◽  
Vol 8 (27) ◽  
pp. 43635-43652 ◽  
Author(s):  
Thuy Linh Nguyen ◽  
Janna Schneppenheim ◽  
Sönke Rudnik ◽  
Renate Lüllmann-Rauch ◽  
Christian Bernreuther ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Functional Characterization ◽  
Lysosomal Membrane ◽  
Lysosomal Membrane Protein

scholarly journals The lysosomal membrane protein LAMP2A promotes autophagic flux and prevents SNCA-induced Parkinson disease-like symptoms in the Drosophila brain

Autophagy ◽  
2018 ◽  
Vol 14 (11) ◽  
pp. 1898-1910 ◽  
Author(s):  
Abdul-Raouf Issa ◽  
Jun Sun ◽  
Céline Petitgas ◽  
Ana Mesquita ◽  
Amina Dulac ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Parkinson Disease ◽  
Lysosomal Membrane ◽  
Autophagic Flux ◽  
Drosophila Brain ◽  
Lysosomal Membrane Protein

Expression of the lysosomal membrane protein LMBD1 is essential for the initiation of gastrulation

2017 ◽  
Vol 120 (1-2) ◽  
pp. S117
Author(s):  
Frank Rutsch ◽  
Petra Pennekamp ◽  
Yvonne Nitschke ◽  
Chrishanthi Lowe ◽  
Boris Skryabin ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Lysosomal Membrane ◽  
Lysosomal Membrane Protein

scholarly journals Rapid transfer of overexpressed integral membrane protein from the host membrane into soluble lipid nanodiscs without previous purification

2015 ◽  
Vol 396 (8) ◽  
pp. 903-915 ◽  
Author(s):  
Nazhat Shirzad-Wasei ◽  
Jenny van Oostrum ◽  
Petra H.M. Bovee-Geurts ◽  
Lisanne J.A. Kusters ◽  
Giel J.C.G.M. Bosman ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Functional Characterization ◽  
Integral Membrane Protein ◽  
Partial Purification ◽  
Functional Studies ◽  
Host Membrane ◽  
Lipid Nanodiscs ◽  
Membrane Scaffold ◽  
Rapid Transfer

Abstract Structural and functional characterization of integral membrane proteins in a bilayer environment is strongly hampered by the requirement of detergents for solubilization and subsequent purification, as detergents commonly affect their structure and/or activity. Here, we describe a rapid procedure with minimal exposure to detergent to directly assemble an overexpressed integral membrane protein into soluble lipid nanodiscs prior to purification. This is exemplified with recombinant his-tagged rhodopsin, which is rapidly extracted from its host membrane and directly assembled into membrane scaffold protein (MSP) nanodiscs. We further demonstrate that, even when the MSP was his-tagged as well, partial purification of the rhodopsin-nanodiscs could be achieved exploiting immobilized-metal chromatography. Recoveries of rhodopsin up to 80% were achieved in the purified nanodisc fraction. Over 95% of contaminating membrane protein and his-tagged MSP could be removed from the rhodopsin-nanodiscs using a single Ni2+-affinity chromatography step. This level of purification is amply sufficient for functional studies. We provide evidence that the obtained rhodopsin-nanodisc preparations are fully functional both photochemically and in their ability to bind the cognate G-protein.

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