Bright on the right feels right: SQUARC compatibility is hedonically marked.

According to the Spatial Quantity Association of Response Codes (SQUARC), people hold a mental association between horizontal position and quantity (lower quantities left, higher quantities right). While a large body of research has explored this effect for response speed and judgment accuracy, the affective downstream consequences of the SQUARC remain unexplored. Aiming to address this gap, the present two experiments (pre-registered, total  = 521) investigated whether stimulus arrangements that are compatible with the SQUARC for luminance are affectively preferred to stimulus arrangements that are incompatible.

1H, 13C, and 15N chemical shift assignments for the Eps15-EH2-stonin 2 complex.

EH domains are protein-protein interaction domains that function in vesicular trafficking and endocytosis. Here, we report the NMR spectral assignments of the high-affinity complex between the second EH domain of Eps15 and a stonin 2 peptide--providing the basis for the characterization of a two-site binding mode.

Isoform-selective interaction of the adaptor protein Tks5/FISH with Sos1 and dynamins.

The adaptor protein Tks5/FISH (tyrosine kinase substrate 5/five SH3 domains, hereafter termed Tks5) is a crucial component of a protein network that controls the invasiveness of cancer cells and progression of Alzheimer's disease. Tks5 consists of an amino-terminal PX domain that is followed by five SH3 domains (SH3A-E), and two different splice variants are expressed. We identified son of sevenless-1 (Sos1) as a novel binding partner of Tks5 and found colocalization of Tks5 with Sos1 in human epithelial lung carcinoma (A549) cells and in podosomes of Src-transformed NIH 3T3 cells.

Structure of the Eps15-stonin2 complex provides a molecular explanation for EH-domain ligand specificity.

Eps15 homology (EH) domain-containing proteins play a key regulatory role in intracellular membrane trafficking and cell signalling. EH domains serve as interaction platforms for short peptide motifs comprising the residues NPF within natively unstructured regions of accessory proteins. The EH-NPF interactions described thus far are of very low affinity and specificity.