Here we show, using X-ray crystallographic, biochemical and EM experiments, that a widespread family of conserved bacterial proteins, the linocin-like proteins, form large assemblies that function as a minimal compartment to package enzymes.
It is also known that endocytic vesicles can function as a signaling compartment distinct from the plasma membrane [60].
Evidence that transcriptional regulators such as p53, CBP and Daxx are transiently targeted and retained in PML bodies suggests that they function as a storage compartment and thus regulate pathways involved in tumor suppression, viral defense and apoptosis [ 12].
It was recently suggested that pathogenic mutations in dysferlin result in improper folding of the protein and therefore in dysfunction and degradation.[57] Moreover, it has been shown that the ER can function as an intracellular storage compartment of recombinant dysferlin [58], which is in line with elongated translation/folding time.
Hence, once it is translocated into the nucleus and desumoylated, it could potentially function as a catalyst in this compartment for some time.
Indeed, this Bem3-containing compartment functioned as a recycling station that was present at the junction of endocytic and secretory pathways and required actin tracks for trafficking to polarized sites.
Tau protein is enriched in the axonal compartment, where it functions as a regulator of microtubule dynamics.
DOI: http://dx.doi.org/10.7554/eLife.01641.011 A second hypothesis suggested that Ki-67 might function as a scaffolding platform for organising the perichromosomal compartment.
Recent studies also reveal that zinc can be stored and released from intracellular vesicular compartments and can function as a novel intracellular second messenger [3], [4].
Concomitantly, it functions as a filter and establishes communication between both compartments (Bazzoni 2006).
The structural features of p76 suggest that it may function as a channel or small molecule transporter in intracellular compartments throughout phylogeny.
