News

Sysmic Annual Meeting

Sysmic will hold its annual meeting January 9-10, 2019 in Uppsala. Registration should be made to Staffan Strömblad before December 18.

Sysmic researchers have identified mechanism for amoeboid cell migration

Xiaowei Gong and his colleagues in the Strömblad laboratory identified a role for RhoB in cell mebrane blebbing and amoeboid cell migration in a recently published study. The role of RhoB is linked to its subcellular localization where RhoB can be recycled to the plasma membrane and there serve to promote blebbing and thereby promote cell migration. This recycling occurs through Rab11-positive vesicles and is dependent on KIF13A.

Publication: Gong X, Didan Y, Lock JG, Strömblad S. KIF13A-regulated RhoB plasma membrane localization governs membrane blebbing and blebby amoeboid cell migration. EMBO J. 2018 Sep 3;37(17). pii: e98994. doi: 10.15252/embj.201898994. Epub 2018 Jul 26.

New cell adhesion structure discovered

John Lock and his colleagues in the Strömblad laboratory, in collaboration with researchers in Manchester, UK, has discovered a novel cellular structure in the form of Reticular adhesions, an cell-matrix adhesion structure with a unique componentry. The researchers also found that the Reticular adhesions mediate cell attachment during mitotic round-up, when all previously know adhesion structures disassemble. Given the central role of cell-matrix adhesion in mesenchymal cell migration, the Reticular adhesions may also affect cell migration, but this remains to be examined.

Publication:  Lock JG, Jones MC, Askari JA, Gong X, Oddone A, Olofsson H, Göransson S, Lakadamyali M, Humphries MJ, Strömblad S. Reticular adhesions are a distinct class of cell-matrix adhesions that mediate attachment during mitosis. Nat Cell Biol. 2018 Nov;20(11):1290-1302. doi: 10.1038/s41556-018-0220-2. Epub 2018 Oct 22.

 

The nanoscale organization of cell-matrix contact receptors unraveled

Cell-matrix contact points such as focal adhesions are critical for cell migration. In a study published in The Journal of Cell Biology, Staffan Strömblad and colleagues used superresolution microscopy to, for the first time, characterize the nanoscale organization of integrin cell-matrix receptors within focal adhesions. Surprisingly, they found that active (matrix-bound) and inactive (unbound) 1-integrins segregate into distinct nanoclusters within the focal adhesions, suggesting the existence of a novel mechanism for collective integrin activity regulation