@article{7875,
  abstract     = {Cells navigating through complex tissues face a fundamental challenge: while multiple protrusions explore different paths, the cell needs to avoid entanglement. How a cell surveys and then corrects its own shape is poorly understood. Here, we demonstrate that spatially distinct microtubule dynamics regulate amoeboid cell migration by locally promoting the retraction of protrusions. In migrating dendritic cells, local microtubule depolymerization within protrusions remote from the microtubule organizing center triggers actomyosin contractility controlled by RhoA and its exchange factor Lfc. Depletion of Lfc leads to aberrant myosin localization, thereby causing two effects that rate-limit locomotion: (1) impaired cell edge coordination during path finding and (2) defective adhesion resolution. Compromised shape control is particularly hindering in geometrically complex microenvironments, where it leads to entanglement and ultimately fragmentation of the cell body. We thus demonstrate that microtubules can act as a proprioceptive device: they sense cell shape and control actomyosin retraction to sustain cellular coherence.},
  author       = {Kopf, Aglaja and Renkawitz, Jörg and Hauschild, Robert and Girkontaite, Irute and Tedford, Kerry and Merrin, Jack and Thorn-Seshold, Oliver and Trauner, Dirk and Häcker, Hans and Fischer, Klaus Dieter and Kiermaier, Eva and Sixt, Michael K},
  issn         = {1540-8140},
  journal      = {The Journal of Cell Biology},
  number       = {6},
  publisher    = {Rockefeller University Press},
  title        = {{Microtubules control cellular shape and coherence in amoeboid migrating cells}},
  doi          = {10.1083/jcb.201907154},
  volume       = {219},
  year         = {2020},
}

@article{1599,
  abstract     = {The addition of polysialic acid to N- and/or O-linked glycans, referred to as polysialylation, is a rare posttranslational modification that is mainly known to control the developmental plasticity of the nervous system. Here we show that CCR7, the central chemokine receptor controlling immune cell trafficking to secondary lymphatic organs, carries polysialic acid. This modification is essential for the recognition of the CCR7 ligand CCL21. As a consequence, dendritic cell trafficking is abrogated in polysialyltransferase-deficient mice, manifesting as disturbed lymph node homeostasis and unresponsiveness to inflammatory stimuli. Structure-function analysis of chemokine-receptor interactions reveals that CCL21 adopts an autoinhibited conformation, which is released upon interaction with polysialic acid. Thus, we describe a glycosylation-mediated immune cell trafficking disorder and its mechanistic basis.
},
  author       = {Kiermaier, Eva and Moussion, Christine and Veldkamp, Christopher and Gerardy  Schahn, Rita and De Vries, Ingrid and Williams, Larry and Chaffee, Gary and Phillips, Andrew and Freiberger, Friedrich and Imre, Richard and Taleski, Deni and Payne, Richard and Braun, Asolina and Förster, Reinhold and Mechtler, Karl and Mühlenhoff, Martina and Volkman, Brian and Sixt, Michael K},
  journal      = {Science},
  number       = {6269},
  pages        = {186 -- 190},
  publisher    = {American Association for the Advancement of Science},
  title        = {{Polysialylation controls dendritic cell trafficking by regulating chemokine recognition}},
  doi          = {10.1126/science.aad0512},
  volume       = {351},
  year         = {2016},
}

@article{1618,
  abstract     = {CCL19 and CCL21 are chemokines involved in the trafficking of immune cells, particularly within the lymphatic system, through activation of CCR7. Concurrent expression of PSGL-1 and CCR7 in naive T-cells enhances recruitment of these cells to secondary lymphoid organs by CCL19 and CCL21. Here the solution structure of CCL19 is reported. It contains a canonical chemokine domain. Chemical shift mapping shows the N-termini of PSGL-1 and CCR7 have overlapping binding sites for CCL19 and binding is competitive. Implications for the mechanism of PSGL-1's enhancement of resting T-cell recruitment are discussed.},
  author       = {Veldkamp, Christopher and Kiermaier, Eva and Gabel Eissens, Skylar and Gillitzer, Miranda and Lippner, David and Disilvio, Frank and Mueller, Casey and Wantuch, Paeton and Chaffee, Gary and Famiglietti, Michael and Zgoba, Danielle and Bailey, Asha and Bah, Yaya and Engebretson, Samantha and Graupner, David and Lackner, Emily and Larosa, Vincent and Medeiros, Tysha and Olson, Michael and Phillips, Andrew and Pyles, Harley and Richard, Amanda and Schoeller, Scott and Touzeau, Boris and Williams, Larry and Sixt, Michael K and Peterson, Francis},
  journal      = {Biochemistry},
  number       = {27},
  pages        = {4163 -- 4166},
  publisher    = {American Chemical Society},
  title        = {{Solution structure of CCL19 and identification of overlapping CCR7 and PSGL-1 binding sites}},
  doi          = {10.1021/acs.biochem.5b00560},
  volume       = {54},
  year         = {2015},
}

@article{1686,
  author       = {Kiermaier, Eva and Sixt, Michael K},
  journal      = {Science},
  number       = {6252},
  pages        = {1055 -- 1056},
  publisher    = {American Association for the Advancement of Science},
  title        = {{Fragmented communication between immune cells: Neutrophils blaze a trail with migratory cues for T cells to follow to sites of infection}},
  doi          = {10.1126/science.aad0867},
  volume       = {349},
  year         = {2015},
}