C1 domain mediates CalDAGIII localization to the Golgi.
CalDAGs are a family of Ras guanyl exchange factors that contain calcium and DAG-binding domains. Among the four identified members of CalDAG family, CalDAGIII has been shown to play important role in B lymphocyte and endocrine cell functions. However, the mechanism underlining these functions remain to be determined. Here in the present study, we determined the subcellular localization of CalDAGIII and roles of calcium-binding and DAG-binding domains in its localization. We found that C1 domain but not EF hands is important for both CalDAGIII localization to the Golgi and p38 activation in B cells, indicating that CalDAGIII may be regulated by DAG but not calcium.
Zhang
Mingyu
M
Department of Cardiology, The 4th Affiliated Hospital of Harbin Medical University, 150001, Harbin, Peoples Republic of China.
Xia
Hongyuan
H
Li
Xueqi
X
Wang
Xiaoyun
X
Dong
Yumei
Y
Zhang
Tong
T
Yu
Hongwei
H
D001402:B-Lymphocytes / Q000378:metabolism; D020832:EF Hand Motifs; D004789:Enzyme Activation; D006056:Golgi Apparatus / Q000378:metabolism*; D020662:Guanine Nucleotide Exchange Factors / Q000737:chemistry* / Q000378:metabolism*; D057809:HEK293 Cells; D006801:Humans; D018613:Microscopy, Confocal; D050505:Mutant Proteins / Q000737:chemistry / Q000378:metabolism; D017434:Protein Structure, Tertiary; D021381:Protein Transport; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D015398:Signal Transduction; D013329:Structure-Activity Relationship; D048051:p38 Mitogen-Activated Protein Kinases / Q000378:metabolism
D020662:Guanine Nucleotide Exchange Factors; D050505:Mutant Proteins; D011993:Recombinant Fusion Proteins; D048051:p38 Mitogen-Activated Protein Kinases