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Hua Jin
Hua Jin, PhD
Assistant Professor
UIC Biological Sciences, MBRB 4120, M/C 567
900 South Ashland Ave.
Chicago, IL 60607

Office: (312) 413-8137
Email: huajin@uic.edu

Dr. Jin's lab web site

The primary cilium is a microtubule based, solitary and non-motile organelle that projects from cell body. The primary cilium houses signaling receptors and their downstream targets, and therefore serves as an antenna and signaling hub for the cell. Primary cilia are present in almost all the cells in our body including neuronal cells. Fascinatingly, primary cilium dysfunction leads to a group of human hereditary disorders whose clinical features include retinal degeneration, polycystic kidney, polydactyly, obesity and psychiatric disorders.

The primary goals in the Jin lab are to unravel how signaling receptors traffic in and out of the primary cilia, how trafficking impinge upon cellular signaling, and to relate these understandings to the molecular basis of defects in various diseases.

To achieve these goals, we use a multiplicity of experimental approaches that range from electron microscopy, in vitro cell-free systems, mouse genetics, protein complex purification and advanced light microscopy of heterologous system, mammalian cell lines and primary neuron cultures.

Representative Publications

Jin H, White SR, Shida T, Schulz S, Aguiar M, Gygi SP, Bazan JF, Nachury MV. (2010) The conserved Bardet-Biedl Syndrome proteins assemble a coat that traffics membrane proteins to cilia. Cell 141(7): 1208-1219. (cover story)

2. Hu Q, Milenkovic L, Jin H, Scott MP, Nachury MV, Spiliotis ET, Nelson WJ. (2010) A septin diffusion barrier at the base of the primary cilium maintains ciliary membrane protein distribution. Science 329: 436 - 439.

3. Nachury MV, Seeley ES, Jin H. (2010) Trafficking to the ciliary membrane: How to get across the periciliary diffusion barrier? Annu. Rev. Cell Dev. Biol. 26: 59-87.

4. Jin H, Hong Z, Su W, Li J. (2009) A plant-specific calreticulin is a key retention factor for a defective brassinosteroid receptor in the endoplasmic reticulum. Proc Natl Acad Sci U S A 106(32):13612-7.

5. Hong Z, Jin H, Fitchette AC, Xia Y, Monk AM, Faye L, and Li J. (2009) Mutations of an {alpha}1,6 mannosyltransferase inhibit endoplasmic reticulum-associated degradation of defective brassinosteroid receptors in Arabidopsis. Plant Cell 21:3792-3802.

6. Hong Z*, Jin H*, Tzfira T, Li J. (2008) Multiple mechanism-mediated retention of a defective brassinosteroid receptor in the endoplasmic reticulum. Plant Cell 20: 3418-3429. (*: equal contribution)

7. Jin H, Yan Z, Nam KH, Li J. (2007) Allele-specific suppression of a defective brassinosteroid receptor reveals a physiological role of UGGT in ER quality control. Molecular Cell 26(6): 821-830.