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TitleStructural basis of microtubule-mediated signal transduction.
Journal, issue, pagesCell, Year 2025
Publish dateDec 8, 2025
AuthorsSung Ryul Choi / Thorsten B Blum / Matteo Giono / Bibhas Roy / Ioannis Vakonakis / Dominic Schmid / Nicole Oelgarth / Apisha Ranganathan / Alvar D Gossert / G V Shivashankar / Alfred Zippelius / Michel O Steinmetz /
PubMed AbstractMicrotubules have long been recognized as upstream mediators of intracellular signaling, but the mechanisms underlying this fundamental function remain elusive. Here, we identify the structural basis ...Microtubules have long been recognized as upstream mediators of intracellular signaling, but the mechanisms underlying this fundamental function remain elusive. Here, we identify the structural basis by which microtubules regulate the guanine nucleotide exchange factor H1 (GEFH1), a key activator of the Ras homolog family member A (RhoA) pathway. We show that specific features of the microtubule lattice bind the C1 domain of GEFH1, leading to the sequestration and inactivation of this signaling protein. Targeted mutations in C1 residues disrupt this interaction, triggering GEFH1 release and activation of RhoA-dependent immune responses. Building on this sequestration-and-release mechanism, we identify microtubule-binding C1 domains in additional signaling proteins, including other guanine nucleotide exchange factors (GEFs), kinases, a GTPase-activating protein (GAP), and a tumor suppressor, and show that microtubule-mediated regulation via C1 domains is conserved in the Ras association domain-containing protein 1A (RASSF1A). Our findings establish a structural framework for understanding how microtubules can function as spatiotemporal signal sensors, integrating and processing diverse signaling pathways to control important cellular processes.
External linksCell / PubMed:41365297
MethodsEM (single particle) / NMR (solution)
Resolution2.74 - 3.4 Å
Structure data

51768

9h1o

EMDB-51768, PDB-9h1o:
Cryo-EM structure of taxol-microtubules in complex with the C1 domain of GEFH1
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-54112: CryoEM structure of the microtubule-AKAP13 C1 domain complex
Method: EM (single particle) / Resolution: 2.74 Å

PDB-9h75:
NMR solution structure of the GEFH1 C1 domain
Method: SOLUTION NMR

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM

ChemComp-TA1:
TAXOL / medication, chemotherapy*YM

Source
  • homo sapiens (human)
  • bos taurus (domestic cattle)
  • Sus scrofa (pig)
KeywordsSIGNALING PROTEIN / RhoGEF / C1 / Cytoskeleton / Complex / PROTEIN BINDING / STRUCTURE FROM CYANA 3.98.4

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