The clathrin assembly protein PICALM is required for erythroid maturation and transferrin internalization in mice

Phosphatidylinositol binding clathrin assembly protein (PICALM), also known as clathrin assembly lymphoid myeloid leukemia protein (CALM), was originally isolated as part of the fusion gene CALM/AF10, which results from the chromosomal translocation t(10;11)(p13;q14). CALM is sufficient to drive cla...

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Veröffentlicht in:	PloS one 2012-02, Vol.7 (2), p.e31854-e31854
Hauptverfasser:	Suzuki, Mai, Tanaka, Hirokazu, Tanimura, Akira, Tanabe, Kenji, Oe, Natsuko, Rai, Shinya, Kon, Syunsuke, Fukumoto, Manabu, Takei, Kohji, Abe, Takaya, Matsumura, Itaru, Kanakura, Yuzuru, Watanabe, Toshio
Format:	Artikel
Sprache:	eng
Schlagworte:	Adaptor Proteins, Vesicular Transport - metabolism Anemia Anemia - pathology Animals Assembly Biology Bone marrow Budding Cell Differentiation Clathrin Cloning Crosses, Genetic Dentistry Embryo fibroblasts Embryo, Mammalian - cytology Endocytosis Erythroblasts - cytology Erythroblasts - metabolism Erythroid cells Erythroid Cells - cytology Erythroid Cells - metabolism Female Fibroblasts Fibroblasts - cytology Fibroblasts - metabolism Flow Cytometry Fusion protein Gene Targeting Genetic engineering Genotype Hematology Hematopoiesis Humanities Immunoglobulins In vivo methods and tests Internal medicine Internalization Iron Iron - metabolism Iron content Leukemia Lipid monolayers Liver transplants Longevity Male Maturation Medicine Membrane vesicles Mice Mice, Inbred C57BL Mice, Knockout Monomeric Clathrin Assembly Proteins Monomolecular films Mutation Myeloid leukemia Neurosciences Pharmaceutical sciences Phosphatidylinositol Physiological aspects Protein binding Proteins Stem cell transplantation Transferrin Transferrin - metabolism Transferrins Translocation Tumors University graduates Women
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Zusammenfassung:	Phosphatidylinositol binding clathrin assembly protein (PICALM), also known as clathrin assembly lymphoid myeloid leukemia protein (CALM), was originally isolated as part of the fusion gene CALM/AF10, which results from the chromosomal translocation t(10;11)(p13;q14). CALM is sufficient to drive clathrin assembly in vitro on lipid monolayers and regulates clathrin-coated budding and the size and shape of the vesicles at the plasma membrane. However, the physiological role of CALM has yet to be elucidated. Here, the role of CALM in vivo was investigated using CALM-deficient mice. CALM-deficient mice exhibited retarded growth in utero and were dwarfed throughout their shortened life-spans. Moreover, CALM-deficient mice suffered from severe anemia, and the maturation and iron content in erythroid precursors were severely impaired. CALM-deficient erythroid cells and embryonic fibroblasts exhibited impaired clathrin-mediated endocytosis of transferrin. These results indicate that CALM is required for erythroid maturation and transferrin internalization in mice.
ISSN:	1932-6203 1932-6203
DOI:	10.1371/journal.pone.0031854