If Sar1 is inserted into the ER membrane: O It is bound to GDP and recruits COPII coat proteins O It is not bound to any nucleotide O It is bound to GTP and recruits cargo O It is bound to GTP and recruits COPII coat proteins O It is bound to GTP and recruits clathrin coat proteins

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**Question:**

If Sar1 is inserted into the ER membrane:

- ○ It is bound to GDP and recruits COPII coat proteins
- ○ It is not bound to any nucleotide
- ○ It is bound to GTP and recruits cargo
- ○ It is bound to GTP and recruits COPII coat proteins
- ○ It is bound to GTP and recruits clathrin coat proteins

**Explanation:**

When Sar1, a small GTPase, is inserted into the endoplasmic reticulum (ER) membrane, it typically interacts with various other proteins and molecules in a specific manner depending on the nucleotide to which it is bound. This process is crucial for the transport of proteins from the ER to the Golgi apparatus, especially during vesicle formation.

**Options Explained:**

- **Bound to GDP and recruits COPII coat proteins:** This option is incorrect because, when Sar1 is bound to GDP, it doesn’t actively recruit COPII proteins.
  
- **Not bound to any nucleotide:** This scenario is highly unlikely, as Sar1 usually functions by binding either GTP or GDP.

- **Bound to GTP and recruits cargo:** This partially explains Sar1's activity, but it primarily acts to recruit coat proteins.

- **Bound to GTP and recruits COPII coat proteins:** This is the correct answer. When Sar1 binds to GTP, it changes shape, allowing it to insert into the ER membrane and recruit COPII coat proteins, which are essential for vesicle budding.

- **Bound to GTP and recruits clathrin coat proteins:** This is incorrect because clathrin is involved in a different pathway, typically in endocytosis, not in ER to Golgi transport. 

Understanding these mechanisms is vital for insights into intracellular trafficking and protein sorting.
Transcribed Image Text:**Question:** If Sar1 is inserted into the ER membrane: - ○ It is bound to GDP and recruits COPII coat proteins - ○ It is not bound to any nucleotide - ○ It is bound to GTP and recruits cargo - ○ It is bound to GTP and recruits COPII coat proteins - ○ It is bound to GTP and recruits clathrin coat proteins **Explanation:** When Sar1, a small GTPase, is inserted into the endoplasmic reticulum (ER) membrane, it typically interacts with various other proteins and molecules in a specific manner depending on the nucleotide to which it is bound. This process is crucial for the transport of proteins from the ER to the Golgi apparatus, especially during vesicle formation. **Options Explained:** - **Bound to GDP and recruits COPII coat proteins:** This option is incorrect because, when Sar1 is bound to GDP, it doesn’t actively recruit COPII proteins. - **Not bound to any nucleotide:** This scenario is highly unlikely, as Sar1 usually functions by binding either GTP or GDP. - **Bound to GTP and recruits cargo:** This partially explains Sar1's activity, but it primarily acts to recruit coat proteins. - **Bound to GTP and recruits COPII coat proteins:** This is the correct answer. When Sar1 binds to GTP, it changes shape, allowing it to insert into the ER membrane and recruit COPII coat proteins, which are essential for vesicle budding. - **Bound to GTP and recruits clathrin coat proteins:** This is incorrect because clathrin is involved in a different pathway, typically in endocytosis, not in ER to Golgi transport. Understanding these mechanisms is vital for insights into intracellular trafficking and protein sorting.
Expert Solution
Step 1: Introduction

Sar1 is a small GTPase that plays a key role in the formation of COPII vesicles, which transport proteins from the ER to the Golgi apparatus.

Sar1 is bound to the ER membrane by a transmembrane domain at its C-terminus. When Sar1 is bound to GDP, it is inactive. However, when Sar1 binds to GTP, it becomes active and recruits COPII coat proteins to the ER membrane. The COPII coat proteins then help to assemble COPII vesicles.

Once the COPII vesicle is assembled, Sar1 hydrolyzes GTP to GDP and becomes inactive again. This allows the COPII vesicle to detach from the ER membrane and be transported to the Golgi apparatus.

Sar1 is an essential protein for cell survival. Mutations in the Sar1 gene can lead to a variety of diseases, including congenital disorders of glycosylation (CDGs) and familial hypercholesterolemia.

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