February 12, 2013

The endoplasmic reticulum (ER) is my kind of organelle for its dynamic nature and sorting abilities.  If you could see my pantry, desk, or closet then you’d know that a life of sorting and organizing is my jaaaaam.  Today’s image is from a paper identifying a regulator of ER dynamics.

The endoplasmic reticulum (ER) is a dynamic, interconnected network of membrane vesicles, cisternae (sac-like structures), and tubules.  The ER serves many functions, including protein synthesis (on the rough ER), protein folding, and protein sorting.  The ER experiences complex rearrangements, and a recent paper identifies Rab10 as a regulator of these ER dynamics.  Rab10 is a Rab GTPase, a family of membrane proteins that function as molecular switches for many membrane-based events such as vesicle formation and fusion.  English and Voeltz found that Rab10 is found on the ER and on ER-structures involved in new ER tubule growth.  Depletion of Rab10, or expression of a mutant Rab10, caused a disruption of ER morphology, as well as reduced ER tubule extension and fusion.  In the images above, cells were labeled with an ER marker.  Compared to controls cells, Rab10-depleted cells had an altered ER morphology, notably more expansive cisternae and fewer tubules.

English, A., & Voeltz, G. (2012). Rab10 GTPase regulates ER dynamics and morphology Nature Cell Biology, 15 (2), 169-178 DOI: 10.1038/ncb2647 
ResearchBlogging.orgAdapted by permission from Macmillan Publishers Ltd, copyright ©2013

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