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Abstract:TM9 proteins form a family of conserved proteins with nine transmembrane domains essential for cellular adhesion in many biological systems, but their exact role in this process remains unknown. Here we found that in Dictyostelium amoebae, genetic inactivation of the TM9 protein Phg1A dramatically decreases the surface levels of the SibA adhesion molecule. This is due to a decrease in sibA mRNA levels, in SibA protein stability, and in SibA targeting to the cell surface. A similar phenotype was observed in cells devoid of SadA, a protein that does not belong to the TM9 family but also exhibits 9 transmembrane domains and is essential for cellular adhesion. A csA-SibA chimeric protein comprising only the transmembrane and cytosolic domains of SibA and the extracellular domain of csA, a Dictyostelium surface protein, also showed reduced stability and relocalization to endocytic compartments in phg1A knockout cells. These results indicate that TM9 proteins participate in cell adhesion by controlling the levels of adhesion proteins present at the cell surface. | |||||||
Status: | aheadofprint | Type: | Journal article | Source: | PUBMED | PubMed ID: | 22219373 |
Genes addressed in this paper | ||||||||
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phg1A | phg1B | phg2 | sadA | sibA | talA | Topics in this paper | ||
Adhesion | X | X | X | |||||
Mammalian Gene Related | X | |||||||
Strains/Constructs | X | X | X | X | X | X | ||
Cellular Location | X | |||||||
Function/Process | X | X | X | X | ||||
Endocytosis | X | X | ||||||
RNA Levels and Processing | X | |||||||
Regulatory Role | X | X | ||||||
Regulated By | X | |||||||
Mutants/Phenotypes | X | X | X | X | X |