Gia Voeltz

Associate Professor

Photo of Gia Voeltz

Phone: (303) 492-3145
EXT: 2-3145
LAB: 2-5231



Office Location



Ph.D., Yale, 2001


Research Interests:
Organelle biogenesis: the regulation of organelle structure and shape by membrane proteins.

Research Profile:

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?

Selected Publications

The reticulon and DP1/Yop1p proteins form immobile oligomers in the tubular endoplasmic reticulum.
Shibata, Y, Voss, C, Rist, JM, Hu, J, Rapoport, TA, Prinz, WA, and Voeltz, GK J Biol Chem, 283(27):18892-904. 2008

A class of membrane proteins shaping the tubular endoplasmic reticulum.
Voeltz, GK, Prinz, WA, Shibata, Y, Rist, JM, and Rapoport, TA Cell, 124(3):573-86. 2006

ER sliding dynamics and ER-mitochondrial contacts occur on acetylated microtubules.
Friedman, JR, Webster, BM, Mastronarde, DN, Verhey, KJ, and Voeltz, GK J Cell Biol, 190(3):363-75. 2010

A 3D analysis of yeast ER structure reveals how ER domains are organized by membrane curvature.
West, M, Zurek, N, Hoenger, A, and Voeltz, GK J Cell Biol, 193(2):333-46. 2011

Reticulon short hairpin transmembrane domains are used to shape ER tubules.
Zurek, N, Sparks, L, and Voeltz, G Traffic, 12(1):28-41. 2011

Peripheral ER structure and function.
English, AR, Zurek, N, and Voeltz, GK Curr Opin Cell Biol, 21(4):596-602. 2009

Sheets, ribbons and tubules - how organelles get their shape.
Voeltz, GK and Prinz, WA Nat Rev Mol Cell Biol, 8(3):258-64. 2007