Gia Voeltz - Assistant Professor
Ph.D., Yale, 2001
Organelle Biogenesis
In the Voeltz lab, we are interested in how membrane-bound organelles are generated. Most organelles have elaborate yet conserved shapes, which require the structural organization of the membrane bilayer along with its unique set of proteins. Generating and maintaining complex organelle morphologies requires specific proteins and perhaps lipids to stabilize them. It has long been clear that a complex interplay of factors must determine organelle morphology, but how, let alone the proteins responsible, are just starting to be discovered.
We are interested in understanding how the endoplasmic reticulum (ER) is formed. It is a large continuous and singular organelle with many different functions and an elaborate shape made up of several structurally distinct domains. Subdomains of the ER include the nuclear envelope (NE) and an extensive network of tubules and sheets/cisternae found in the peripheral ER (see Figure 1). We recently identified two conserved classes of integral membrane proteins, reticulons and DP1/Yop1, that generate the shape of the ER in eukaryotic cells. Some of the questions that we find most intriguing about ER biogenesis are (1) how can the membrane bilayer be shaped into different structures like tubules, sheets, and stacked cisternae when they are all continuous with each other (2) how is the ER disassembled and reassembled into the correct structure following the cell cycle, and (3) what effect does ER shape have on differentiated and polarized cell morphologies?
Shibata Y, Voeltz GK, Rapoport TA, "Rough sheets and smooth tubules." Cell 126 (2006): 435-9
Voeltz GK, Prinz WA, Shibata Y, Rist JM, Rapoport TA, "A class of membrane proteins shaping the tubular endoplasmic reticulum." Cell 124 (2006): 573-86
Voeltz GK, Rolls MM, Rapoport TA, "Structural organization of the endoplasmic reticulum." EMBO reports 3 (2002): 944-50
Voeltz GK, Ongkasuwan J, Standart N, Steitz JA, "A novel embryonic poly(A) binding protein, ePAB, regulates mRNA deadenylation in Xenopus egg extracts." Genes & development 15 (2001): 774-88