p62(super dok): a constitutively tyrosine-phosphorylated GAP-associated protein in chronic myelogenous leukemia progenitor cells
Article Abstract:
The novel protein p62(super dok) was purified from a hematopoietic cell line expressing the chimeric p210(super bcr-abl) protein which is usually found in chronic myelogenous leukemia. A unique feature of the p62(super dok) protein is the presence of a signaling molecule. Association of p62(super dok) with the GTPase-activating protein correlated with its tyrosine phosphorylation. p62(super dok) is rapidly tyrosine-phosphorylated upon activation of the c-Kit receptor, indicating it to be a component of a signal transduction pathway downstream of receptor tyrosine kinases.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1997
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The p150 and p60 subunits of chromatin assembly factor I: a molecular link between newly synthesized histones and DNA replication
Article Abstract:
The human chromatin assembly factor I(CAF I), is a protein complex having three subunits, p150, p60 and p50, which bind newly synthesized histones onto DNA replication sites indicating that these complexes are intermediates between histone synthesis and assembly onto replicating DNA. In eukaryotic organisms, the DNA is packed in the nucleus with a number of proteins to form a nucleoprotein structure, the chromatin. Of the three subunits in the CAF I protein, p150 and p60 are essential for chromatin assembly activity whereas p50 is uncertain.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
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Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4
Article Abstract:
A chromatin assembly complex (CAC) that contains chromatin assembly factor 1 (CAF-1) and the posttranslationally modified histones H3 and H4 is discovered and characterized. A cDNA for p48, the small subunit of CAF-1 and a member of a highly conserved subfamily of WD-repeat proteins, is cloned. Experiments show that the CAC plays a key role in the de novo nucleosome assembly pathway and that the p48 subunit participates in other aspects of histone metabolism.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
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