Terry Gibbon

Durham University

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Roy A. Quinlan

Durham University

Elly M. Hol

University Medical Center Utrecht

Mu Su

Harbin Institute of Technology

Shu‐Fang Wen

Industrial Technology Research Institute

Michael Brenner

University of Alabama at Birmingham

Jinte Middeldorp

Biomedical Primate Research Centre

Jacqueline A. Sluijs

Utrecht University

Shu Fang Wen

Durham University

Alan R. Prescott

University of Dundee

Rong Li

Affiliated Hospital of North Sichuan Medical College

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Durham University

University Medical Center Utrecht

Utrecht University

Netherlands Institute for Neuroscience

Royal Netherlands Academy of Arts and Sciences

University of Dundee

University Medical Center

University Hospital and Clinics

University of Alabama at Birmingham

National Tsing Hua University

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Glial Fibrillary Acidic Protein Filaments Can Tolerate the Incorporation of Assembly-compromised GFAP-δ, but with Consequences for Filament Organization and αB-Crystallin Association

Molecular Biology of the Cell (2008)

Ming‐Der Perng Shu‐Fang Wen Terry Gibbon Jinte Middeldorp Jacqueline A. Sluijs

The glial fibrillary acidic protein (GFAP) gene is alternatively spliced to give GFAP-α, the most abundant isoform, and seven other differentially expressed transcripts including GFAP-δ. GFAP-δ has an altered C-terminal domain that renders it incapable of self-assembly in vitro. When titrated with GFAP-α, assembly was restored providing GFAP-δ levels were kept low (∼10%). In a range of immortalized and transformed astrocyte derived cell lines and human spinal cord, we show that GFAP-δ is naturally part of the endogenous intermediate filaments, although levels were low (∼10%). This suggests that GFAP filaments can naturally accommodate a small proportion of assembly-compromised partners. Indeed, two other assembly-compromised GFAP constructs, namely enhanced green fluorescent protein (eGFP)-tagged GFAP and the Alexander disease–causing GFAP mutant, R416W GFAP both showed similar in vitro assembly characteristics to GFAP-δ and could also be incorporated into endogenous filament networks in transfected cells, providing expression levels were kept low. Another common feature was the increased association of αB-crystallin with the intermediate filament fraction of transfected cells. These studies suggest that the major physiological role of the assembly-compromised GFAP-δ splice variant is as a modulator of the GFAP filament surface, effecting changes in both protein– and filament–filament associations as well as Jnk phosphorylation.

GFAP stain

10.1091/mbc.e08-03-0284

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The Alexander Disease–Causing Glial Fibrillary Acidic Protein Mutant, R416W, Accumulates into Rosenthal Fibers by a Pathway That Involves Filament Aggregation and the Association of αB-Crystallin and HSP27

The American Journal of Human Genetics (2006)

Ming Der Perng Mu Su Shu Fang Wen Rong Li Terry Gibbon

Intermediate Filament Protein

10.1086/504411

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Citations (121)