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Jianzhong Wen
University of California, San Diego
28Publications
20H-index
2,081Citations
Publications 29
Newest
#1Vincent S. Tagliabracci (UCSD: University of California, San Diego)H-Index: 19
#2Sandra E. Wiley (UCSD: University of California, San Diego)H-Index: 25
Last.Jack E. Dixon (UCSD: University of California, San Diego)H-Index: 102
view all 15 authors...
The existence of extracellular phosphoproteins has been acknowledged for over a century. However, research in this area has been undeveloped largely because the kinases that phosphorylate secreted proteins have escaped identification. Fam20C is a kinase that phosphorylates S-x-E/pS motifs on proteins in milk and in the extracellular matrix of bones and teeth. Here, we show that Fam20C generates the majority of the extracellular phosphoproteome. Using CRISPR/Cas9 genome editing, mass spectrometry...
99 CitationsSource
#1Jack E. Dixon (UCSD: University of California, San Diego)H-Index: 102
#2Vincent S. Tagliabracci (UCSD: University of California, San Diego)H-Index: 19
Last.Nick V. Grishin (UTSW: University of Texas Southwestern Medical Center)H-Index: 78
view all 10 authors...
Protein phosphorylation is a fundamental mechanism regulating nearly every aspect of life. Several secreted proteins are phosphorylated, but the kinases responsible are unknown. We identified a family of atypical protein kinases which have N-terminal signal sequence and localize to the lumen of the endoplasmic reticulum and the Golgi apparatus. One of these kinases known as Fam20C is the Golgi casein kinase and it phosphorylates secretory pathway proteins within S-x-E motifs. Fam20C phosphorylat...
#1Jixin Cui (UCSD: University of California, San Diego)H-Index: 5
#2Junyu Xiao (UCSD: University of California, San Diego)H-Index: 9
Last.Jack E. Dixon (UCSD: University of California, San Diego)H-Index: 102
view all 6 authors...
Some proteins must be modified in order to work effectively. One common modification is to add a phosphate group to the protein, which is performed by enzymes called protein kinases. Although most of the protein kinases work on proteins inside the cell, it was discovered recently that a small group of kinases work within the ‘secretory pathway’ and modify proteins that are released (or secreted) out of cells. One such secretory pathway kinase—called Fam20C—phosphorylates a wide range of secreted...
49 CitationsSource
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Most eukaryotic cells elaborate several proteoglycans critical for transmitting biochemical signals into and between cells. However, the regulation of proteoglycan biosynthesis is not completely understood. We show that the atypical secretory kinase family with sequence similarity 20, member B (Fam20B) phosphorylates the initiating xylose residue in the proteoglycan tetrasaccharide linkage region, and that this event functions as a molecular switch to regulate subsequent glycosaminoglycan assemb...
44 CitationsSource
#1Peter G. Adams (University of Sheffield)H-Index: 10
#2Ashley J. Cadby (University of Sheffield)H-Index: 17
Last.C. Neil Hunter (University of Sheffield)H-Index: 48
view all 9 authors...
Abstract Chlorosomes, the major antenna complexes in green sulphur bacteria, filamentous anoxygenic phototrophs, and phototrophic acidobacteria, are attached to the cytoplasmic side of the inner cell membrane and contain thousands of bacteriochlorophyll (BChl) molecules that harvest light and channel the energy to membrane-bound reaction centres. Chlorosomes from phototrophs representing three different phyla, Chloroflexus (Cfx.) aurantiacus, Chlorobaculum (Cba.) tepidum and the newly discovered...
17 CitationsSource
#1Junyu Xiao (UCSD: University of California, San Diego)H-Index: 9
#2Vincent S. Tagliabracci (UCSD: University of California, San Diego)H-Index: 19
Last.Jack E. DixonH-Index: 102
view all 5 authors...
The family with sequence similarity 20 (Fam20) kinases phosphorylate extracellular substrates and play important roles in biomineralization. Fam20C is the Golgi casein kinase that phosphorylates secretory pathway proteins within Ser-x-Glu/pSer motifs. Mutations in Fam20C cause Raine syndrome, an osteosclerotic bone dysplasia. Here we report the crystal structure of the Fam20C ortholog from Caenorhabditis elegans. The nucleotide-free and Mn/ADP-bound structures unveil an atypical protein kinase-l...
49 CitationsSource
#1Vincent S. Tagliabracci (UCSD: University of California, San Diego)H-Index: 19
#2James L. Engel (UCSD: University of California, San Diego)H-Index: 8
Last.Jack E. Dixon (UCSD: University of California, San Diego)H-Index: 102
view all 9 authors...
Protein phosphorylation is a fundamental mechanism regulating nearly every aspect of cellular life. Several secreted proteins are phosphorylated, but the kinases responsible are unknown. We identified a family of atypical protein kinases that localize within the Golgi apparatus and are secreted. Fam20C appears to be the Golgi casein kinase that phosphorylates secretory pathway proteins within S-x-E motifs. Fam20C phosphorylates the caseins and several secreted proteins implicated in biomineraliz...
253 CitationsSource
#1Hao Zhang (WashU: Washington University in St. Louis)H-Index: 22
#2Jianzhong Wen (WashU: Washington University in St. Louis)H-Index: 20
Last.Michael L. Gross (WashU: Washington University in St. Louis)H-Index: 75
view all 5 authors...
Protein structure determines function in biology, and a variety of approaches have been employed to obtain structural information about proteins. Mass spectrometry-based protein footprinting is one fast-growing approach. One labeling-based footprinting approach is the use of a water-soluble carbodiimide, 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) and glycine ethyl ester (GEE) to modify solvent-accessible carboxyl groups on glutamate (E) and aspartate (D). This paper describes method dev...
25 CitationsSource
#1Richard Y.-C. HuangH-Index: 15
#2Jianzhong WenH-Index: 20
Last.Michael L. GrossH-Index: 75
view all 4 authors...
In green-sulfur bacterial photosynthesis, excitation energy absorbed by a peripheral antenna structure known as the chlorosome is sequentially transferred through a baseplate protein to the Fenna–Matthews–Olson (FMO) antenna protein and into the reaction center, which is embedded in the cytoplasmic membrane. The molecular details of the optimized photosystem architecture required for efficient energy transfer are only partially understood. We address here the question of how the baseplate intera...
29 CitationsSource
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