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Grundmann, L.

Publications and source records attributed to Grundmann, L..

2 recordsLinked to original sources

Unraveling the mystery behind the short-day-specific flowering of tobacco cultivar Maryland Mammoth

Flowering in day-neutral tobacco (Nicotiana tabacum) plants requires the photoperiod-dependent expression of members of the FLOWERING LOCUS T (FT)-like clade of phosphatidylethanolamine-binding proteins. FT-like floral activators and inhibitors compete for interaction with FD proteins to shift from vegetative to reproductive growth. In the short-day (SD) cultivar Maryland Mammoth (MM), vegetative growth persists under long-day (LD) conditions, generating unusually tall plants. We found that the major floral inducer under long-days (NtFT5) was expressed in MM and that NtFT5 overexpression induced flowering in MM plants under LD conditions. However, sequence analysis revealed a 2-bp deletion near the 3 end of NtFT5 in MM plants resulting in a frame shift which leads to an altered amino acid sequence and a premature stop codon. We found that the truncated NtFT5MM protein was still able to interact with tobacco FD proteins. However, constitutive overexpression under LD conditions in SD-specific flowering tobacco plants showed that NtFT5MM is a weaker floral inducer than NtFT5. Our data suggest that the truncation does not impair the stability of the NtFT5MM protein but may affect its binding affinity for NtFD1, probably resulting in the weaker expression of target genes. Our results therefore provide a potential explanation for the MM gigantism phenotype first observed more than 100 years ago. HighlightThe previously unexplained gigantism of Maryland Mammoth tobacco is caused by a truncated major floral activator protein that results in weaker activation and the inability to flower under long-day conditions.

plant biology↗

Quantitative Proteomics Identifies PTP1B as Modulator of B Cell Antigen Receptor Signaling

B cell antigen receptor (BCR) signaling is initiated by protein kinases and limited by counteracting phosphatases that currently are less well studied in their regulation of BCR signaling. We here used the B cell line Ramos to identify and quantify human B cell signaling components. Specifically, a protein tyrosine phosphatase profiling revealed a high expression of the protein tyrosine phosphatase 1B (PTP1B) in Ramos and human naive B cells. The loss of PTP1B leads to increased B cell activation. Through substrate trapping in combination with quantitative mass spectrometry, we identified 22 putative substrates or interactors of PTP1B. We validated Ig, CD22, PLC{gamma}1/2, CBL, BCAP and APLP2 as specific substrates of PTP1B in Ramos B cells. The tyrosine kinase BTK and the two adaptor proteins GRB2 and VAV1 were identified as direct binding partners and potential substrates of PTP1B. We showed that PTP1B dephosphorylates the inhibitory receptor protein CD22 at phosphotyrosine 807. We conclude that PTP1B negatively modulates BCR signaling by dephosphorylating distinct phosphotyrosines in B cell specific receptor proteins and various downstream signaling components.

biochemistry↗