Emp24p is a type I transmembrane protein that is involved in secretory protein transport from the endoplasmic reticulum (ER) to the Golgi complex. A yeast mutant that lacks Emp24p (emp24 delta) is viable, but periplasmic invertase and the glycosylphosphatidyl‐inositol‐anchored plasma membrane protein Gas1p are delivered to the Golgi apparatus with reduced kinetics, whereas transport of alpha‐factor, acid phosphatase and two vacuolar proteins is unaffected. Oligomerization and protease digestion studies of invertase suggest that the selective transport phenotype observed in the emp24 delta mutant is not due to a defect in protein folding or oligomerization. Consistent with a role in ER to Golgi transport, Emp24p is a component of COPII‐coated, ER‐derived transport vesicles that are isolated from a reconstituted in vitro budding reaction. We propose that Emp24p is involved in the sorting and/or concentration of a subset of secretory proteins into ER‐derived transport vesicles.

Abstract. The Saccharomyces cerevisiae EMP47 gene encodes a nonessential type-I transmembrane protein with sequence homology to a class of intracellular lectins defined by ERGIC-53 and VIP36. The 12-amino acid COOH-terminal cytoplasmic tail of Emp47p ends in the sequence KTKLL, which conforms with the consensus for di-lysine-based ER-localization signals. Despite the presence of this motif, Emp47p was shown to be a Golgi protein at steady-state. The di-lysine motif of Emp47p was functional when transplanted onto Ste2p, a plasma membrane protein, conferring ER localization. Nevertheless, the di-lysine motif was required for Golgi-localization of Emp47p and showed the same charge-independent, position-dependent characteristics of other di-lysine motifs.a-COP has been shown to be required for ER localization of di-lysine-tagged proteins. Consistent with this finding, the Ste2p-Emp47p hybrid protein was mislocalized to the cell surface in the oL-COP mutant, retl-1. Surprisingly, the Golgi-localization of Emp47p was unaffected by the retl-1 mutation. To investigate whether Emp47p undergoes retrograde transport from the Golgi to the ER like other di-lysine-tagged proteins we developed an assay to measure this step after block of forward transport in a secl2 mutant. Under these conditions retrograde transport led to a specific redistribution of Emp47p from the Golgi to the ER. This recycling occurred from a Golgi subcompartment containing od,3 mannose-modified oligosaccharides suggesting that it originated from a medial-or later Golgi compartment. Thus Emp47p cycles between the Golgi apparatus and the ER and requires a di-lysine motif for its a-COP-independent, steady state localization in the Golgi.

We demonstrate resistive humidity sensing using a single-layer graphene patch placed on top of a SiO2 layer on a Si wafer.

Nanoelectromechanical system (NEMS) sensors and actuators could be of use in the development of next generation mobile, wearable, and implantable devices. However, these NEMS devices require transducers that are ultra-small, sensitive and can be fabricated at low cost. Here, we show that suspended double-layer graphene ribbons with attached silicon proof masses can be used as combined spring-mass and piezoresistive transducers. The transducers, which are realized using processes that are compatible with large-scale semiconductor manufacturing technologies, can yield NEMS accelerometers that occupy at least two orders of magnitude smaller die area than conventional state-of-the-art silicon accelerometers. With our devices, we also extract the Young's modulus values of double-layer graphene and show that the graphene ribbons have significant built-in stresses.