Till sidans topp

Sidansvarig: Webbredaktion
Sidan uppdaterades: 2012-09-11 15:12

Tipsa en vän
Utskriftsversion

Bcr (breakpoint cluster r… - Göteborgs universitet Till startsida
Webbkarta
Till innehåll Läs mer om hur kakor används på gu.se

Bcr (breakpoint cluster region) protein binds to PDZ-domains of scaffold protein PDZK1 and vesicle coat protein Mint3.

Artikel i vetenskaplig tidskrift
Författare Emily Malmberg
Christian X Andersson
Martina Gentzsch
Jey H Chen
April Mengos
Liying Cui
Gunnar C. Hansson
John R Riordan
Publicerad i Journal of cell science
Volym 117
Nummer/häfte Pt 23
Sidor 5535-41
ISSN 0021-9533
Publiceringsår 2004
Publicerad vid Institutionen för medicinsk och fysiologisk kemi
Sidor 5535-41
Språk en
Länkar dx.doi.org/10.1242/jcs.01472
Ämnesord Amino Acid Sequence, Animals, Carrier Proteins, chemistry, genetics, metabolism, Cell Compartmentation, physiology, Cell Membrane, metabolism, Cricetinae, Cytosol, metabolism, Epithelial Cells, metabolism, Golgi Apparatus, metabolism, secretion, HT29 Cells, Humans, Molecular Sequence Data, Protein Binding, physiology, Protein Structure, Tertiary, physiology, Protein Transport, physiology, Protein-Tyrosine Kinases, metabolism, Proteins, metabolism, Proto-Oncogene Proteins, metabolism, Proto-Oncogene Proteins c-bcr, Respiratory Mucosa, cytology, Transport Vesicles, metabolism
Ämneskategorier Medicin och Hälsovetenskap

Sammanfattning

The breakpoint cluster region protein (Bcr) is a large soluble oligomeric multidomain protein best known because of its involvement in chronic myelogenous leukemia (CML). A chromosomal translocation between its gene and that of the c-abl kinase ('Philadelphia chromosome') plays a major causative role in that malignancy. Thus most attention has been paid to the role of the protein in hemopoietic cells. However, Bcr is also expressed in other cell types including epithelia. Bcr is generally considered to be a cytoplasmic protein but in addition to its kinase and GTPase exchange and activating domains it contains potentially membrane-interacting pleckstrin homology and C2 domains as well as a PDZ-binding C terminus mediating an interaction with a PDZ-domain protein at intercellular junctions of epithelial cells. We have examined the ability of Bcr to interact with other epithelial PDZ proteins and found specific binding to both the apical PDZK1 protein and the Golgi-localized Mint3. The former is important in the organization of several apical functions and the latter in vesicular trafficking in the secretory pathway. Hence these findings extend the interactions and likely signaling impact of Bcr in epithelia from the cytosol to at least these two membrane compartments.

Sidansvarig: Webbredaktion|Sidan uppdaterades: 2012-09-11
Dela:

På Göteborgs universitet använder vi kakor (cookies) för att webbplatsen ska fungera på ett bra sätt för dig. Genom att surfa vidare godkänner du att vi använder kakor.  Vad är kakor?