The Golgi apparatus plays a key role in protein sorting and their post translational modifications. All proteins synthesized in the endoplasmic reticulum and targeted to the plasma membrane, lysosomes or to be secreted in the medium are somehow modified in the Golgi apparatus before they reach their final destination. Such post-translational modifications require the concerted action of numerous enzymes that are selectively localized in the three major sub-compartments of the Golgi, i.e. the Cis- Intermediate and Trans-Golgi. In addition, it has been demonstrated that the Golgi not only can accumulate Ca²⁺ within its lumen in an ATP dependent way, but also that it can release it into the cytoplasm during cell activation. Finally evidence has been provided by different groups indicating that the lumenal Ca²⁺ concentration in the Golgi is pivotal for several of the organelle functions. We have recently demonstrated that the trans-Golgi does not express significant amounts neither of the Sarco-Endoplasmic-Reticulum Ca²⁺ ATPase nor of the IP3 receptors, but rather it is endowed with another Ca²⁺ ATPase, the Secretory Pathway Ca²⁺ ATPase (SPCA1) and ryanodine receptors. Here I will briefly discuss these characteristics of the Trans-Golgi compartment and I will then focus on a few recent results obtained with a new GFP-based Ca²⁺ indicator selectively localized in the Cis- and Intermediate Golgi regions. I will show that these two compartments behave, in terms of Ca²⁺ handling, very differently from the trans Golgi and that within these two subregions the different cysternae appear quite heterogeneous in terms of both IP3 sensitivity and Ca²⁺ uptake mechanisms.