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The endoplasmic reticulum (ER), a cellular organelle that forms acell-spanning network of tubes and sheets, is an important location of proteinsynthesis and folding. When the ER experiences sustained unfolded proteinstress, IRE1 proteins embedded in the ER membrane activate and assemble intoclusters as part of the unfolded protein response (UPR). We use kinetic MonteCarlo simulations to explore IRE1 clustering dynamics on the surface of ERtubes. While initially growing clusters are approximately round, once a clusteris sufficiently large a shorter interface length can be achieved by `wrapping'around the ER tube. A wrapped cluster can grow without further interface lengthincreases. Relative to wide tubes, narrower tubes enable cluster wrapping atsmaller cluster sizes. Our simulations show that wrapped clusters on narrowertubes grow more rapidly, evaporate more slowly, and require a lower proteinconcentration to grow compared to equal-area round clusters on wider tubes.These results suggest that cluster wrapping, facilitated by narrower tubes,could be an important factor in the growth and stability of IRE1 clusters andthus impact the persistence of the UPR, connecting geometry to signalingbehavior. This work is consistent with recent experimental observations of IRE1clusters wrapped around narrow tubes in the ER network.

Tube geometry controls protein cluster conformation and stability on the endoplasmic reticulum surface