| First Author | Chhikara A | Year | 2025 |
| Journal | Cell Rep | Volume | 44 |
| Issue | 10 | Pages | 116290 |
| PubMed ID | 40966085 | Mgi Jnum | J:372749 |
| Mgi Id | MGI:8249727 | Doi | 10.1016/j.celrep.2025.116290 |
| Citation | Chhikara A, et al. (2025) Activity-dependent localization and dynamics of STIM1 and STIM2 at ER-PM contacts in hippocampal neurons. Cell Rep 44(10):116290 |
| abstractText | Stromal interaction molecules (STIMs) are Ca(2+) sensors within the endoplasmic reticulum (ER) plasma membrane (PM) that contribute to homeostatic functions in neurons. Upon depletion of Ca(2+) from the ER, STIMs translocate to ER-PM junctions to contact the inner leaflet of the PM. Using single-particle tracking, we characterize the dynamic properties of endogenous STIM1 and STIM2 proteins in hippocampal neurons. STIMs form clusters in the somato-dendritic compartment but only transiently visit synapses. A substantial fraction of STIM2 proteins define ER-PM contacts under resting conditions and is dependent on the constitutive activity of NMDARs. STIM1 proteins are transiently recruited to ER-PM junctions only during strong activation of NMDARs. Activity-dependent confinement of STIM proteins is not influenced by Ca(V)1.2 channel activity. We propose that STIM proteins fulfill a dominant structural function in neurons by regulating the size and frequency of ER-PM contacts to promote ER-PM communication along dendrites. |
