Schirmer lab paper featured in the Journal of Cell Biology. Image Authors Zuleger N, Kelly DA, Richardson AC, Kerr AR, Goldberg MW, Goryachev AB, Schirmer EC. Summary Using a combination of photoactivation and fluorescence recovery after photobleaching (FRAP) techniques, the Schirmer lab found that most nuclear envelope transmembrane proteins are highly immobile in the nuclear membrane. The figure shows that very little of photoactivated LAP1 has moved within the membrane in 15 minutes. It followed from this that FRAP on the nuclear envelope mostly measured translocation of new proteins from the ER to the inner nuclear membrane. They then used this finding to test several different theories for how membrane proteins translocate to the nucleus while directly comparing many different proteins. This revealed that different sets of nuclear envelope proteins use at least four distinct mechanisms to translocate to the inner nuclear membrane, one of which was first proposed in this work. This paper has already been included among the faculty of 1000 list of important studies. Related links Journal Link FACULTY OF 1000 comment This article was published on 2024-06-17
