Professor | Junmin Pan | Asia Growth Partners

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Name	Junmin Pan
Contact Information	panjunmin@tsinghua.edu.cn
Language ability	English, Chinese, German
Province	Beijing

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Name

Junmin Pan

Contact Information

panjunmin@tsinghua.edu.cn

Language ability

English, Chinese, German

Province

Beijing

University/Lab Affiliation and Title	Tsinghua University
Faculty	Life Sciences
Academic Background & Achievements	1986 Bachelor: Hebei Normal University 1989 Master: Institute of Hydrobiology, Chinese Academy of Sciences 1996 PhD: University of Freiburg, Germany
Work Experience	1997-1999 - USA Southwestern Medical Center - Postdoctoral Researcher 2000-2006 - USA Southwestern Medical Center - Research Assistant Professor 2006-Present - Tsinghua University School of Life Sciences - Professor
Awards	Vice Chairman of the Chinese Phycological Society Vice Chairman of the Cell Structure and Behavior Branch of the Chinese Society for Cell Biology Review Editor at eLife

University/Lab Affiliation and Title

Tsinghua University

Faculty

Life Sciences

Academic Background & Achievements

1986 Bachelor: Hebei Normal University
1989 Master: Institute of Hydrobiology, Chinese Academy of Sciences
1996 PhD: University of Freiburg, Germany

Work Experience

1997-1999 - USA Southwestern Medical Center - Postdoctoral Researcher
2000-2006 - USA Southwestern Medical Center - Research Assistant Professor
2006-Present - Tsinghua University School of Life Sciences - Professor

Awards

Vice Chairman of the Chinese Phycological Society
Vice Chairman of the Cell Structure and Behavior Branch of the Chinese Society for Cell Biology
Review Editor at eLife

Areas of Focus	Ciliary Biology Microalgae Technology Development and Utilization
Publications	IFT54 directly interacts with kinesin-II and IFT dynein to regulate anterograde intraflagellar transport, Zhu X, Wang J, Li S, Lechtreck K, Pan J, 2021 Functional exploration of heterotrimeric kinesin-II in IFT and ciliary length control in Chlamydomonas, Li S, Wan KY, Chen W, Tao H, Liang X, Pan J, 2020 FLS2 Is a CDK-like Kinase That Directly Binds IFT70 and Is Required for Proper Ciliary Disassembly in Chlamydomonas, Zhao Q, Li S, Shao S, Wang Z, Pan J, 2020 Ciliary Length Sensing Regulates IFT Entry via Changes in FLA8/KIF3B Phosphorylation to Control Ciliary Assembly, Liang Y, Zhu X, Wu Q, Pan J, 2018 Functional exploration of the IFT-A complex in intraflagellar transport and ciliogenesis, Zhu B, Zhu X, Wang L, Liang Y, Feng Q, Pan J, 2017 Cilia disassembly with two distinct phases of regulation, Hu J, Liang Y, He W, Pan J , 2015 FLA8/KIF3B phosphorylation regulates kinesin-II interaction with IFT-B to control IFT entry and turnaround, Liang Y, Pang Y, Wu Q, Hu Z, Han X, Xu Y, Deng H, Pan J, 2014 Activation loop phosphorylation of a protein kinase is a molecular marker of organelle size that dynamically reports flagellar length, Cao M, Meng D, Wang L, Bei S, Snell WJ, Pan J, 2013

Areas of Focus

Ciliary Biology
Microalgae Technology Development and Utilization

Publications

IFT54 directly interacts with kinesin-II and IFT dynein to regulate anterograde intraflagellar transport, Zhu X, Wang J, Li S, Lechtreck K, Pan J*, 2021
Functional exploration of heterotrimeric kinesin-II in IFT and ciliary length control in Chlamydomonas, Li S, Wan KY, Chen W, Tao H, Liang X*, Pan J*, 2020
FLS2 Is a CDK-like Kinase That Directly Binds IFT70 and Is Required for Proper Ciliary Disassembly in Chlamydomonas, Zhao Q, Li S, Shao S, Wang Z, Pan J*, 2020
Ciliary Length Sensing Regulates IFT Entry via Changes in FLA8/KIF3B Phosphorylation to Control Ciliary Assembly, Liang Y, Zhu X, Wu Q, Pan J*, 2018
Functional exploration of the IFT-A complex in intraflagellar transport and ciliogenesis, Zhu B, Zhu X, Wang L, Liang Y, Feng Q, Pan J*, 2017
Cilia disassembly with two distinct phases of regulation, Hu J, Liang Y, He W, Pan J *, 2015
FLA8/KIF3B phosphorylation regulates kinesin-II interaction with IFT-B to control IFT entry and turnaround, Liang Y, Pang Y, Wu Q, Hu Z, Han X, Xu Y, Deng H, Pan J*, 2014
Activation loop phosphorylation of a protein kinase is a molecular marker of organelle size that dynamically reports flagellar length, Cao M, Meng D, Wang L, Bei S, Snell WJ*, Pan J*, 2013

Ciliary Movement Signal Transduction Structural Defects Human Diseases Assembly Disassembly Protein Transport Genetic Transcription Chlamydomonas Animal Cells

Junmin Pan - Tsinghua University

Jia-Jia Liu - University of Chinese Academy of Sciences

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